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secY

Gene
SECY
Protein
Preprotein translocase subunit SECY, chloroplastic
Organism
Oryza sativa subsp. japonica
Length
556 amino acids
Function
The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug (By similarity).
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
59.53 kDa
Sequence
MAAMATPQQCWLPTRARAPPPPPPRAPSSASPVSGAPASLRFRGRRAASASASAARRRRGASLPCSPRCALETAGPGFDPLGLYNDGPSRNDTQSPLSNFFGVLSPVFGSSSGGRKEKSYGRGAAAAIEDSSIDIGDFFKGPLPGKFLKLLGYLALSRLGIYIPLGGVNRDAFAGNLDQNSLLGTLDSFSGGGIGRLGICSLGIVPFINAQIVFQLLAQLYPKLQDLQKKEGEAGRKKVLQYTRYASVGFAIVQAIGQVLFLRPYVNDFSTEWVLTSVTLLTLGSVFTTFIGERISDLKLGNGTSLLIFTSIISYLPASFGRTVAQAFQDGNYVGLLTIILSFLFLVLGIVYVQEAERKIPLNYASRYSSRSGGLQRSAYLPFKVNSSGVMPIIFSTSSLALPGTLARFTGLEFLKKAAISLNPGGALYIPTNVLLIAFFNYYYTFLQLDPDDLSEQLKRQGASIPLVRPGKSTAAFIKTVLSNISVLGSAFLAVLAAGPSVVEQITHLTAFRGFAGTSVLILVGCATDTARKVQAEIISQKYKNIEFYDVNRFDQ

Gene
SECY
Protein
Preprotein translocase subunit SECY, chloroplastic
Organism
Zea mays
Length
553 amino acids
Function
The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug (By similarity).
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
59.354 kDa
Sequence
MVTATTTPPQCWRGLPALARAPPPLSSPLRPRAVAAAAPIYPLRRRIAITTTRGRRGTLDCSPRCTLETAGPGFDPLGLYEEGSNSLSRSPLSTFFGIMAPVFGSSSGGGASREKASGRGAAAAIEDSSIDIGDFFKGPLPGKFLKLLGFLALSRLGVYIPLGGVNREAFAGNLDQNSLLGTLDSFSGGGIGRLGICSLGIVPFINAQIVFQLLAQLYPKLQDLQRKEGEAGRKKVLQYTRYASVGFAIVQAIGQVLYLRPYVNDFSTEWVLTSVTLLTLGSVFTTFIGERISDLKLGNGTSLLIFTSIISYLPASFGRTVAQAFQDGNYVGLLTIILSFLLLVLGIVYVQEAERKIPLNYASRYSSRTGELQRSAYLPFKVNSSGVMPIIFSTSSLALPGTLARFSGLDFLKKAAIALNPGGALYLPTNVLLIAFFNYYYTFLQLDPDDLSEQLKRQGASIPLVRPGKSTAAYIKTVLNRISVLGSAFLAVLAAGPSLVEQTSHLTAFRGFAGTSVLILVGCATDTARKVQAEIISQKYKNIEFYDVNRFGQ

Gene
SECY
Protein
Preprotein translocase subunit SECY, chloroplastic
Organism
Spinacia oleracea
Length
545 amino acids
Function
The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug (By similarity).
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
58.501 kDa
Sequence
MLVTFTEAAATASTSSLISFSLSSPPKFHHKSRIYGCKATFGLRTKPTSWIAAASLSSSTTTTSSCGSSVFDPLGIEQDNSWGVASAWDGVLKFVSQTFESSSGTRKDRSSSARGVAAAIEDSSIDFGDFFKGPLPGKFLTLLGLLALSRLGIYVPLGGVNREAFVGNLDQNSFISTLDSFSGGGIGRLGICSLGIVPFINAQIVFQLLSQVYPKLQDLQKKEGEAGRKKIKQYTQYASVGFALVQAIGQVLFLRPYVNDYSTEWVLSSVILLTLGSVFTTYLGERISDLKLGNGTSLLIFTNIISYLPASFGRTVAEAYQEGNYTGLAIIVVSFVSLVFGIVYVQEAERKIPMNYASRYSGKSGGLQKSAYLPFKVNSAGVMPIIFSTSSLSLPATLARFTGLDILKKAAVALTPGGSFYLPTNILLIAFFNYYYTFLQLDPDDVSEQLKRQGASIPLVRPGKSTAAYIKTVLSRISVLGSGFLAILAAGPAVVEQATHLTAFRGFAGTSVLILVGCATDTARKVQAELISQKYKNIEFYDLEK

Gene
SECY
Protein
Preprotein translocase subunit SECY, chloroplastic
Organism
Pisum sativum
Length
527 amino acids
Function
The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug (By similarity).
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
57.556 kDa
Sequence
MLITVRDPSPTLRCSSLNRRLIPTKHNLSPRLLRSSFRQHNLSLRLRSSSSSNLYTSCDLANFDPLGINPDLSSSSTWRNLLTIFQTSSQKDKPRGVAAAIEDSSIDFGDFFNGPLPGKFLKLLGFLALSRLGVYIPLGGVNRDAFLGNLDQNSLLTTLDSFSGGGIGRLGICSLGIVPFINAQIVFQLLAQVYPKLQDLQKKEGEAGRKKLLQYTRYASVGFAIVQAIGQVLFLRPYANDFTTEWALTSVILLTLGSVFTTYIGEQITELKLGNGTSLLIFTNIISYLPASFGRTFSQAFSDANYVGLVTIIVSFFLLVLGIVYVQEAERKIPINYASRFTSKSGGIEKSAYLPFKVNSSGVMPIIFSTSSLALPGTLARFTGLSSLKTAAVALNPGGSFYLPFNILLIAFFNYYYTFLQLDPDDVSEQLKRQGASIPLVRPGKSTATFIKTVLSRISVLGSTFLAILAAGPAVVEQTAHLTAFRGFAGTSILILVGCATDTARKVRAEIISQKYKNIELYDFDKY

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
Length
498 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
55.045 kDa
Sequence
MAKTNSKNLLGQKIIKLLRNRDFVISVFVTLFLILLFRVISVIPLPGITISQNKNNLNNGVSDFFDLFNLLGGGGLSQLSLFAVGISPYISAQIIMQLLSTDLIPPLSKLAKSGELGRRRIELITRFVTLPFAVVQAFAIIALINNQRNGAIRFENGGILHQAFYIVTMTAGTYIGIFIGDIISKKGVGNGITLLILSGILARLPDGFIVMYRVLGGVIISTNPILTSAINFSLYFLAFLVLLLAISFVNSSTRRIPIQQTGEGMVLGNEKLPYLPIKLNAAGVIPVIFASSIMSIPITIAEFQPQSEARWFVEDYLSLRTPVGISLYVILIIIFTFFYSYIQINPEQLAENFNKSHKFIPGVRPGLDTEKHITKVLMRINFIGAPFLAIVAVIPYIISLVLNVPTTLSLGGTGIIIMVSASMELYRSLRSAATTTSYQRLRKDIANRIEAELSLNDYMNKPNLEHDQYGLLGQHKKVEPTQDKKKNPSDPLEVSQLW

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Length
493 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
53.351 kDa
Sequence
MDSVIRALQPYFERIPSVERPKGHVHFREKFGWTAAILLLYFILSNVPVFGLSPESIDIFAAYRALFAGSTGSIIALGIGPIVTASIILQLLVGAGIIKLDLTNPEDRAAYQDFQRFLVFVMIAVEAIPQIAGGLLKPDLNLAAQLGVSPGIISFLIFIQLFIGGVLIVYMDEVVSKWGIGSGVSLFILAGIAQSIVVGLFNWVIPPNSAMPAGIIPRWIWIAQNYPLDQLFTGSGLAFLLIQGGILALITTAAIILLVVFFEGTRVEIPLAHAVARGARGRFPIKLIYASVLPMIFVRALQANVVALGQVLHARGVTIFGEFVNGKAVSGLMFFLQPVSSPYDWIPSLVKSQGAAFAAIPDWMIYLHLLIDALILVVGGIIFAWFWVETSGMDARTVASQIAKSGMQVPGFRKSPQVLERVLSRYIPKVTILGGAIIGILTLVANMLGTIGNVSGTGLLLAVSIAYRFYEDLAKEQLTEMHPLIRRMLGEEA

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Cyanophora paradoxa
Length
492 amino acids
Function
The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug (By similarity).
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
55.927 kDa
Sequence
MLSRLIISIFIIFETIYLQIFKPVNKTFKQGEAKLKRTLQTLQSRELSEIRKRAISTLCLIFLIRIGTFLPIPGTALNFDLESFQQNNSRNELANILNLLSGGAFLEIGFFTLGILPYMNASFFLQVLTKILPSLERFQKEQEEIAQREFKKWTRYLTVIWAFIQSIVISWIWIRPYALNWDFFLGLKVVVALTLGAVIVMIIAEQITEIGLTNGSSLLIFINIIARIPNSIEQLFNSNINWTFPMISSLILSLSLSFITMFVIIGLQESGRPVPVLIARQEAERQKFNEPITEAERRKTQAYIFFQLLPAGIMPVIFASTIFDLALPAFTNFLLQQGNWGYQLIKSFPFNSLFKDFCYLITIMLFSSNYALTIMINPKTLAENLNSMNALIPGVRPGSETKVYSEQLIHRLNFIGSFVLALVCILPSIVERSLGLPKLQILSPVSISIALGVAVDTTRRITSYLGSSSPFKRDSSKREPLKRDFSKRRSAN

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
Length
491 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
52.819 kDa
Sequence
MGWKEAAAPVLTRMPAVERPEGHVPFRRKMYWTGGVLVLYFFLTNVPLWGIQTAGNDFFGQFRSLLAGGQGTVLQLGIGPIVTASIVLQLLGGANLLGLDTDNDPRDQAIYQGLQKFLVGVMVVLTGAPMVFLGNFLQPSQQLAQSMPGGAFGVEVLIFAQIAAGGILLLFMDEVISKWGVGSGIGLFIVAGVSQSLVGGLVFWEGGVGSQGLLPTWFDIIVGNVSNMPPLLSGSGIEFLLMQAGILGLLTTLFIYVVVVYAESVRVEIPLSHARVKGARGRFPVKLIYASVLPMILVRALQANIQFLGQILNSTLASMPTWLGVYGGNGQVTGGLFYYLAPIYSPNAWMWWTSGATAARWQVLIRIAIDLSFMIIGGAIFAIFWVETADMGPDATARQIQNSGMQIPGFRKNQGVIEKVMERYIPQVTVIGGALVGLLAVMANMLGTIGNVSGTGLLLTISITYKLYEEIAEEQMMEMHPMMREMFGGGD

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)
Length
489 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
52.325 kDa
Sequence
MGWKDAAEPVLSRMPAVARPEGHVPFRRKLGWTGGILVLYFFLTNVTLFGLDAATANDLFGQFRSILAGQQGSVLQLGIGPIVTASIVLQLLGGADLLGLDTDNNPRDQVLYQGLQKLLVGVMICLTGLPMVFAGNFLPADQAVATSLGIGTVGVKGLIFAQIAVGGVLILFMDEIVSKWGVGSGVGLFIIAGVSQQLVGGLFSWQGLGGTSGFFATWIGIITGAIELPASPTDLLSTVFLGQGQLLALITTLLIFGIVVYAESVRVEIPLSHARVKGARGRFPVKLIYASVLPMILVRALQANIQFLGRFLNSSWVGMPAWLGQYTSGQVTGGLLYYLAPIQSRSDWMWFLGLTSADPLDIAIRVLIDLIFMIVGGAVFAIFWVETTGMGPKSTAQQIQNSGMQIPGFRRNPQVIERVMERYIPQVTVIGGALVGLLAVMANMLGTIGAVSGTGLLLTVSITYKLYEEIAEEQLMEMHPMMRNMFGSE

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
Length
487 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
52.533 kDa
Sequence
MSWKDTAEPLLVRMPAVQRPEGHVPFKRKLTWTGGVLLLYFFLTNVKLFGLDIDASQQVFGRFSSILASGQGSIMQLGIGPIVTASIVLQLLGGADLLGLNTQDDPRDQILYQGLQKLLVLVMICLTGLPMVFAGGFLPADTAVANSLGIGTAGVQWLIFAQMFVGGVLILFMDEVISKWGVGSGIGLFIVAGVSQRLVGGLLTAPFLGNSEGIIYTWYLFITGERGTGPVLAADGLQTVLLQGELLGLFTTVLIFAVVVYAESVRVEIPLSNARVKGARGRFPVKLIYASVLPMILVRALQANIQFLGRILNAQLGSMPAFLGTYANGQPTGGLFYFLAPIQSRGDWMWWLEGTAQPVWQILTRVGIDLFVMLVGGAVFAVFWVETTDMGPEATAKQIHNSGMQIPGFRQNVGVIEKVLERYIPQVTVIGGALVGLLAVMANMLGTIGGVSGTGLLLTVSITYKLYEEIAEEQLMEMHPMMRQMFG

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 / NCTC 10154)
Length
482 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
53.315 kDa
Sequence
MVIKKPANKVDKKSTFKSSNKKKNPFKSSFLTKNKDLIYRILFTLLALIIIRLGVYITVPGVTLDKRFATDSSRIQFFQLLSTLGGGSIGRFSILALGVSPYITASIIVQLLSTDVIPVLTRWSKSGERGRKKLDKLTKIIMIPFALMQAEATIFTLSSQGLIIPGWDNTNAIANSAFYYILIPLVMLGGSFFMLWIADQITIKGIGNGISIVIFIGIIISMPSNLKSTFEYWVSNSGEEANIFFSGLLNFMIYISVFLLVILSVVIMNEAERKIPIQQTGSGLTDSSEHTPYLPLKLNNAGVIPVIFASAIISTPITISQIIEAVNPDSGFVIFTRDYLSFNTWWGISIFGILIVLFTFLYSQVQINPEKIAENFQKSGTFIPGIKPGKDTTKYLTGIINRLSVVGSVFLAIIALLPYVISKLTQLPSNLAIGGTGLIICISVAIQTVQQLKGRIIQQNFIEKKKEKFTNNINKNKTSHIW

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Mycoplasma pneumoniae (strain ATCC 29342 / M129)
Length
477 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
51.967 kDa
Sequence
MQAKPTTAVKQKQNFGQRLFTLLRNRDFMISFLITVVLLVLFRVLAIIPLPGIQVNQTGLDQNSNDFFSLFNLLGGGGLNQLSLFAVGISPYISAQIVMQLLSTDLIPPLSKLVNSGEVGRRKIEMITRIITLPFALVQSFAVIQIATNSGGGSSPITLKNNGSDFVAFYIIAMTAGTYLSVFLGDTISKKGIGNGITLLILSGILAQLPEGFIAAYSVLSGVVVTINATLTTAISFFIYFMAFVTLLFATTFITQETRKIPIQQSGQGLVTESSALPYLPIKVNSAGVIPVIFASSIMSIPVTIAQFQPQTESRWFVEDYLSLSKPTGIVLYGILVILFSFFYSYIQINPERLAKNFEKSGRFIPGIRPGKDTEKHIARVLVRINFIGAPFLTVIAIIPYIVSALIHLPNSLSLGGTGIIIIVTAVVEFMSALRSAATATNYQQLRRNLAIEVQKTAQQDKEEQLRAETPGIGNLW

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195)
Length
475 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
51.845 kDa
Sequence
MQTVSSPKQKLNFGQRLLTLLQNRDFMVSLVLTVVLLILFRVLAIIPLPGIRINESVLDRNSNDFFSLFNLLGGGGLNQLSLFAVGISPYISAQIIMQLLSTDLIPPLSKLVNSGEVGRRKIEMITRIITLPFALVQAFAVIQIATNAGTGSSPISLANSGSEFIAFYIIAMTAGTYMAVFLGDTISKKGVGNGITLLILSGILSQLPQGFIAAYNVLSGIVITLTPQLTAAISFFIYFLAFLVLLFATTFITQATRKIPIQQSGQGLVSEVKTLPYLPIKVNAAGVIPVIFASSIMSIPVTIAQFQPQTESRWFVEDYLSLSTPVGIFLYAVLVILFSFFYSYIQINPERLAKNFEKSGRFIPGIRPGNDTEKHIARVLIRINFIGAPFLTVIAIIPYIVSYFIRLPNSLSLGGTGIIIIVTAVVEFISALRSAATATNYQQLRRNLAIEVQQTAKQDSLEQLQKEAPGIGNLW

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Length
469 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
50.493 kDa
Sequence
MSFIDSLATLGQYLPAVTKPKEKPSLGQKLVWSLVAVIIYLIMASTPLYGITSASFFKNLILEQIIFASTTGTLAQLGIGPIITAGLIMQILAGSKLISIDLNDPDDRVKFTEAQKGLAFIFILVESALFGYVLARTSTTINASILFIAGIVIAQLIVATYLILLLDELIQKGWGLGSGVSLFILAGVMKIMFWDMFGIASVSSQNLPIGFFPALFTALASHSDVLNLIVNTSTKNLFQPDLVGLVTTIALIIITIYLTTMTIEIPVTSQKLRGIRRTIPLNFLYVSSIPVIFVAVLGSDIQLFASLASYVSPSASNILNTVSGVFFFPPPNSAIPHSIYAVVLDPLGALEYAVVFIVLSILFGILWVDVAGLDPATQAQQLVEAGIEIPGVRNNPKIIEGILARYIYPLAFFSSIIVGLIAVFATLLGAYGTGIGILLAVTIAIQYYSLLAYERSLEMYPLLKRLIGE

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Pyrococcus abyssi (strain GE5 / Orsay)
Length
468 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
52.157 kDa
Sequence
MGARDIIYAIEKWFPEVERPKKHVPLKEKFMWTGLALILYYVLAEIPVYGIPERIQDYFQFLRVVLAGRNGSILTLGIGPIVTAGIILQLLVGSEIIKLDLANPEDRRFYQALQRVFSVFMCFLEAAIWVLGGAFGRVGVDVTYAIAALMILQLAFGGIILIVLDELVSKWGIGSGISLFIAAGVSQRILTRSLNPLTDPNIIDPLTGKPAIVGAIPYFIQHILKGDLKGALYRGGTAPDMMAVIATIIVFLVVVYFESMRVEIPLGYRGVTIRGRYPIRFLYVSNIPIILTFALYANIQLWARVLDRLGHPWLGTFDPTTGNPVGGFVLYVIPPRSIFTVIDNPVRALVYLILTVISSLIFGFLWVELTGLDARTIARQLQRAGLQIPGFRRDPRTLERVLQKYIPYVTFWGSLTVALIAVLADFLGALGTGTGILLTVGILYRFYEEIAREQISEMFPALRRFFAT

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Length
468 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. Complements an E.coli temperature-sensitive secY mutation; deletion of the last 15 residues prevents complementation, which may indicate a role of this region in translocation.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
52.299 kDa
Sequence
MGARDIIYALERWFPEVERPKRRVPLRERFMWTGVALILYYVLAEIPVYGIPERIQDYFQFLRVVLAGRNGSILTLGIGPIVTAGIILQLLVGSEIIKLDLANPEDRRFYQALQRVFSVFMCFFEAAVWILGGAFGRVGVDVTYAIAVLMILQLAMGGIVLIILDELVSKWGIGSGISLFIAAGVSQTILTRSLNPLTDPNIIDPLTGQPAIVGAIPYFIQHILKGDLWGAIYRGGSAPDMLSVVATIVVFFIVVYFESMRVEIPLGYRGVTVRGSYPIRFLYVSNIPIILTFALYANIQLWARVLDRLGHPWLGRFDPTTGSPISGFVLYVIPPRNIFSVIDNPVRAIVYLILTVIFSLLFGYLWVELTGLDARSIARQLQRAGLQIPGFRRDPRTLEKVLQRYIPYVTFWGSLTVALIAVLADFLGALGTGTGILLTVGILYRFYEEIAREQITEMFPALRKLFGA

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Length
468 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
52.314 kDa
Sequence
MGARDVIYAMEKWFPEVERPKKHVPLKEKFVWTGLALVLYYVLAEIPVYGIPKKIQDYFQFLRVVLAGRNGSILTLGIGPIVTAGIILQLLVGSELIRLDLANPEDRRFYQALQRVFSVFMCFFEAAIWVLGGAFGRVGVDVTYTIATLMIIQLALGGIILIVLDELVSKWGIGSGISLFIAAGVSQRILTRSLNPLTDPNIIDPLTGKPAIVGAIPYFIQHILDGDLKGALYRGGSAPDMIAVTATIIVFLVVVYFESMRVEIPLGYRGVTIRGRYPIKFLYVSNIPIILTFALYANIQLWARVLDRFGHPWLGRFDPVTGNPIGGFVLYVIPPRNIFTVIDNPVRAIIYLILTIIFSLLFGFLWVELTGLDARTIARQLQRAGLQIPGFRRDPRTLERVLQKYIPYVTFWGSLTVALISVLADFLGALGTGTGILLTVGILYRFYEEIAREQITEMFPALRRLFKG

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Length
463 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
50.242 kDa
Sequence
MGFMDFLAKMGENLPAVSKPKDKPTLTRKLLWTFIGLIVYLLMASIPLYGVTSSNSFLSNFLAQQIIFASSQGTLAQLGIGPVITSGLIMQILVGSKLINVDLTTQEGKSKFTQAEKALALIFIIVESSLFGYVFTRATSNILLPIIVVVQLIIASYIILLLDEMIQKGWGLGSGVSLFIMAGIMKVIFWNMFGIVSVQSQNLPVGFFPLLVSYITSGRNLQEIVLNTSSTTPYQPDLIGLIATVGLTILIVYLVNTNIYIPVTTQRLRGIRTTVPLNFLYVSSIPVIFVSVLGADIQLFASLANSISNSASGILTDIANAFFFPPQGVPHSVYALVVDPVGAAIYAAVFIVLSIVFGMLWIDVAGLDPKTQAEQMIRSGIEIPGMRTNPRIIEGILSKYIYALGFFSSLIVGLIAVVATFLGTYGTGVGLLLAITIAMQYYNLLAYERTLEMYPLLKRIVGE

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Length
457 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
49.901 kDa
Sequence
MGVIDVLAAVGERFPAVRKPERKPTLYRRLAWTGVILVLYFIMSNIPLYGIPPQNIGGQVDLQRIIFASSAGTLMELGIGPIVTASLIIQVLVGAKIIKLDLADPEGRRKFTSAQKVLALAFAALEAVAFTVGGRYWVGTAIEPGPLDYALVSLQLFLGALLVIYFDEVMQKGWGIGSAISLFILAGVAQGVVWSIFGTIPGVAQDYGLVPAIISNPDLTLLARPNGFPDLTGFFTTLAAIILLVYLQAMRVEIPITSERFKGIRSRVPLQFIYVTNIPILLVGILVSDLLLVQRLLADYLGVESRAYQIYSSIVYYLSPPRGVVQSIADPVKTAVFIASWTVLSIVFGYMWVEIAGLNPREQAERLIKGGLAIPGMRSDPRVLERVLRRYIYPLTFLSSLIVAALVIVADIFGAYGTGTGLLLAVGIINQYYAMITRERALETYPLLRRILGEEVV

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Chlamydia muridarum (strain MoPn / Nigg)
Length
457 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
50.265 kDa
Sequence
MATLRQVFSISELRQKIFFTFSLLALCRIGVFIPVPGINGDRAVAYFNQLLGSSQNLFQLADIFSGGAFAQMTVIALGVVPYISASIIVQLLVVFMPTLQREMREAPDQGKRKLGRMTRLFTLLLACVQSLLFAKFALRMNLVVPGIVLPAMLSLKLFGIPCVFYLTTVVVMTTGTLLLMWIGEQISDKGIGNGISLIITLGMLASFPSVLGSIFNKLNLGSQDPSEFGIVSLLVLCAVFVFVLMATVLIIEGVRKVPVQHARRIIGRREVLGGGSYLPLKVNYAGVIPVIFASSLLMFPATIGQFLSSESSWLKRIATMLSPGSVVYSIFYVLLIIFFTYFWTATQFRPEQIASEMKKNGAFIPGIRQGKPTQSYLEYTMNRVTLLGAVFLAVVAILPSILGRILRVDANVSYFLGGTAMLIVVGVVLDTMKQIDAFLLVRRYDGVLKKDRPKGRR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Chlamydia pneumoniae
Length
457 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
50.286 kDa
Sequence
MTTLRQFFLITELRQKLFYTFALLTACRVGVFIPVPGINGELAVAYFKQLLGSGQNLFQLADIFSGGAFAQMTVIALGVVPYISASIIVQLFLVFMPALQREMRESSDQGKRRIGRLTRLFTVALAVIQSLLFAKFALRMNLTIPGIVLPTLLSSKLFGVPWIFYITTVVVMTTGTLLLMWIGEQISDKGIGNGISLIIALGILSSFPSVLGSIVNKLNLGSQDSSDLGLISILILALVFVFVLITTILIIEGVRKIPVQYARRVIGRREVPGGGSYLPLKVNYAGVIPVIFASSLLMFPATIGQFIASESSWMKRIAALLAPGSLVYSICYVLLIIFFTYFWTATQFHPEQIASEMKKNNAFIPGIRQGKPTQHYLEYTMNRVTLLGALFLAAIAILPSLLGCLLRVDSNVSYFLGGTAMLIVVGVVLDTMKQVDAFLLMRRYDSVLKTDRTKGRH

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Chlamydia trachomatis (strain D/UW-3/Cx)
Length
457 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
50.303 kDa
Sequence
MATLRQVFSISELRQKIFFTFSLLALCRIGVFIPVPGINGDRAVAYFNQLLGSSQNLFQLADIFSGGAFAQMTVIALGVVPYISASIIVQLLVVFMPTLQREMRESPDQGKRKLGRMTRLFTLVLACVQSLLFAKFALRMNLVVPGIVLPAMLSLKLFGVPWVFYLTTVVVMITGTLLLMWVGEQISDKGIGNGISLIITLGILASFPSVLGSIFNKLNLGSQDPSEFGIVSLLILCAVFVFVLMATVLIIEGMRKIPVQHARRIIGRREVVGGGSYLPLKVNYAGVIPVIFASSLLMFPATIGQFLSSESSWLKRIATMLSPGSVAYSIFYVLLIIFFTYFWTATQFRPEQIASEMKKNGAFIPGIRQGKPTQTYLEYTMNRVTLLGAVFLAVVAILPSILGRILRVDANVSYFLGGTAMLIVVGVILDTMKQIDAFLLVRRYDGVLKKDRPKGRP

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Length
456 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
49.79 kDa
Sequence
MEQLKEKFEPLFSVLPQVKSPGYRVPFREKLKWTGIILVLYFFLAQIPLYGLSANAVDQFAQFRAVLAGNFGSILTLGIGPIVSASIILQLLVGGKILKLDLSRHEDKAFFQGLQKLLAIVFTFFEALIFVLTGSLAPSAPQFVWVLILQLTIGGILIIFLDEVVSKWGFGSGVGLFIAAGVSQEIIVGAFNPLSAPTQPGVPAGRITGFLYLLFTGQSPDFQYYVLPVLALIAVFLVVVYAESMRVEIPISMGGGKRLSRGAVGKYPLRFIYASNMPVILTSALLLNVQLLANVFQKLGYPILGTVSNGQAVDGLAYLLTAPRSIDALILDPFRVVFYAVVFIGLCVLFAWLWVEISNIGPRHVARQLYQMGMQIPGFRSSRGQFEKILKRYIPTITILGGAFVGLLAFVADLTGSLGGGTGVLLTVGIVYRLYEEIAQEQLMDMHPILRSFLGD

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Heterosigma akashiwo (strain NIES-293)
Length
454 amino acids
Function
The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
50.963 kDa
Sequence
MTLEKNKDSFTNIIDLSLINKEQKVTFTPTKEIYTELLKKRLLTIALLVFIIKIGMAIPLPYIDQTKLLNNATSMFDLSGPGLAAVSARASQKIGLFTLGITPSINASIILQLAFVINPNLKKLQREEGESGRRKLIKYTRYLTLLLAITQSVFLIFSLRAFIFEWSILKLFELSCVLSSGAMIILWISECITKTGITNGSSFLIFLNIVSVLPEQIGMSFKNLDIFSFEGLIVILTFSITVWAAIFLQQTLYIIPLKNPKLGQNELTKKLVEDSLYLPFRLNQAGVMPVVFASYLIPILKTGGIYILLKINSFNLFPFLIKFPEVVNQSLESIVEAGLICLFALFYSGLIIDPKDVADELQKSGFFIFAIRPGEKTRNYLEKIFKELSLIGALILAFNVVLLNLVGFVFNLSIFKGFSIGSQIILLGVVTEILQKVQALVLNDVYKRIRDRNK

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Length
444 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
48.664 kDa
Sequence
MARKPGQDFRSAQSGLSELKSRLFFVIGALLVFRAGSFVPIPGIDAAVLAELFEQQKGTIVEMFNMFSGGALERASILALGIMPYISASIVVQLLTVVHPALAELKKEGEAGRRKISQYTRYGTLVLATFQAIGIATGLPNMVNNLVVIDQTMFTLIATVSLVTGTMFLMWLGEQITERGIGNGISILIFAGIVAGLPKAIGQTIEQARQGELHVLLLLLIAVLAFAVIYFVVFMERGQRRIVVNYAKRQQGRKVFAAQSTHLPLKINMAGVIPAIFASSIILFPGTLAQWFGQNGESSTFGWLTDVSLALSPGQPLYVMLYAAAIIFFCFFYTALVFNPRETADNLKKSGAFVPGIRPGEQTAKYIDKVMTRLTLAGALYITFICLIPEFMMVAWNVRFYFGGTSLLIVVVVIMDFMAQVQTHLMSHQYESVLKKANLKGYGR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Escherichia coli O157:H7
Length
443 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
48.512 kDa
Sequence
MAKQPGLDFQSAKGGLGELKRRLLFVIGALIVFRIGSFIPIPGIDAAVLAKLLEQQRGTIIEMFNMFSGGALSRASIFALGIMPYISASIIIQLLTVVHPTLAEIKKEGESGRRKISQYTRYGTLVLAIFQSIGIATGLPNMPGMQGLVINPGFAFYFTAVVSLVTGTMFLMWLGEQITERGIGNGISIIIFAGIVAGLPPAIAHTIEQARQGDLHFLVLLLVAVLVFAVTFFVVFVERGQRRIVVNYAKRQQGRRVYAAQSTHLPLKVNMAGVIPAIFASSIILFPATIASWFGGGTGWNWLTTISLYLQPGQPLYVLLYASAIIFFCFFYTALVFNPRETADNLKKSGAFVPGIRPGEQTAKYIDKVMTRLTLVGALYITFICLIPEFMRDAMKVPFYFGGTSLLIVVVVIMDFMAQVQTLMMSSQYESALKKANLKGYGR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Length
443 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
48.512 kDa
Sequence
MAKQPGLDFQSAKGGLGELKRRLLFVIGALIVFRIGSFIPIPGIDAAVLAKLLEQQRGTIIEMFNMFSGGALSRASIFALGIMPYISASIIIQLLTVVHPTLAEIKKEGESGRRKISQYTRYGTLVLAIFQSIGIATGLPNMPGMQGLVINPGFAFYFTAVVSLVTGTMFLMWLGEQITERGIGNGISIIIFAGIVAGLPPAIAHTIEQARQGDLHFLVLLLVAVLVFAVTFFVVFVERGQRRIVVNYAKRQQGRRVYAAQSTHLPLKVNMAGVIPAIFASSIILFPATIASWFGGGTGWNWLTTISLYLQPGQPLYVLLYASAIIFFCFFYTALVFNPRETADNLKKSGAFVPGIRPGEQTAKYIDKVMTRLTLVGALYITFICLIPEFMRDAMKVPFYFGGTSLLIVVVVIMDFMAQVQTLMMSSQYESALKKANLKGYGR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Escherichia coli (strain K12)
Length
443 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. SecY is required to insert newly synthesized SecY into the inner membrane. Overexpression of some hybrid proteins has been thought to jam the protein secretion apparatus resulting in cell death; while this may be true, overexpression also results in FtsH-mediated degradation of SecY.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
48.512 kDa
Sequence
MAKQPGLDFQSAKGGLGELKRRLLFVIGALIVFRIGSFIPIPGIDAAVLAKLLEQQRGTIIEMFNMFSGGALSRASIFALGIMPYISASIIIQLLTVVHPTLAEIKKEGESGRRKISQYTRYGTLVLAIFQSIGIATGLPNMPGMQGLVINPGFAFYFTAVVSLVTGTMFLMWLGEQITERGIGNGISIIIFAGIVAGLPPAIAHTIEQARQGDLHFLVLLLVAVLVFAVTFFVVFVERGQRRIVVNYAKRQQGRRVYAAQSTHLPLKVNMAGVIPAIFASSIILFPATIASWFGGGTGWNWLTTISLYLQPGQPLYVLLYASAIIFFCFFYTALVFNPRETADNLKKSGAFVPGIRPGEQTAKYIDKVMTRLTLVGALYITFICLIPEFMRDAMKVPFYFGGTSLLIVVVVIMDFMAQVQTLMMSSQYESALKKANLKGYGR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Shigella flexneri
Length
443 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
48.512 kDa
Sequence
MAKQPGLDFQSAKGGLGELKRRLLFVIGALIVFRIGSFIPIPGIDAAVLAKLLEQQRGTIIEMFNMFSGGALSRASIFALGIMPYISASIIIQLLTVVHPTLAEIKKEGESGRRKISQYTRYGTLVLAIFQSIGIATGLPNMPGMQGLVINPGFAFYFTAVVSLVTGTMFLMWLGEQITERGIGNGISIIIFAGIVAGLPPAIAHTIEQARQGDLHFLVLLLVAVLVFAVTFFVVFVERGQRRIVVNYAKRQQGRRVYAAQSTHLPLKVNMAGVIPAIFASSIILFPATIASWFGGGTGWNWLTTISLYLQPGQPLYVLLYASAIIFFCFFYTALVFNPRETADNLKKSGAFVPGIRPGEQTAKYIDKVMTRLTLVGALYITFICLIPEFMRDAMKVPFYFGGTSLLIVVVVIMDFMAQVQTLMMSSQYESALKKANLKGYGR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Length
442 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.832 kDa
Sequence
MAKQGALSALSNGGLSELWARLRFLFLAIIVYRIGAHIPVPGINPDRLAALFRQNEGTILSLFNMFSGGALERMSIFALGIMPYISASIIMQLMTAISPQLEQLKKEGESGRRKISQYTRYGTVVLALVQAIGMSVGLGSQGVAFSNDFGFYFVAVTTFVAGAMFMMWLGEQITERGVGNGISMLIFAGIVAGLPRAIGQSFESARQGDINIFALIGVGLLAVAIIAFVVFIERGQRRIAVHYAKRQQGRKVFAAQTSHLPLKVNMAGVIPAIFASSILLFPASLGSWFGQSEGLGWLQDVAQAIAPGQPLNILLFTAGIVFFCFFYTALMFNPKDVAENLKKSGAFIPGIRPGEQSARYIDGVLTRLTMFGALYMTAVCLLPQFLVVAAHVPFYLGGTSLLIVVVVVMDFMAQVQSHLVSHQYESLMKKANLKGYGSGMLR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Length
442 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
48 kDa
Sequence
MVVSRDKAPSAQETFLQMAQAAGLRGRLLITIGLLILVRVGIFIPVPDIDRQAFSQAINDNSVIGFLNIFTGGGLSTVGIFALGILPYINASIIMQLLTAAIPALEDLQKNEGEAGRRKISQYSRYIAFGWCIIQGLGLTVGLLRPYANNYGPLFIFQTVLAITAGSMFVMWISELITERGIGNGASLLIFVNIVATLPQTLGQTIEYAQSGGRQSITAVVLLMLVFLVMIVGIVFVQEGTRRIPIISARRQVGKKLYRERTSYLPLRLNQGGVMPIIFASAVLILPSSLAGFATGNEGLGGFGEIFVQISNALRPGTWVYTVVYSVMIFFFSYFYASLIVNPEDVSKNLKKMGSSIPGIRPGKKTEQYLEGVLNRLTFLGAIFLSFVATLPIFVEQATGVTTFQGLGATSLLILVGVAIDTAKQIQTYVISQRYEGMIKQP

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Length
441 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.611 kDa
Sequence
MLSAFISSLRTVDLRRKILFTLGIVILYRVGAALPSPGVNFPNVQQCIKEASAGEAGQIYSLINLFSGGALLKLTVFAVGVMPYITASIIVQLLTVVIPRFEELRKEGQAGQSKMTQYTRYLAIALAILQATSIVALAANGGLLQGCSLDIIADQSIFTLVVIVLVMTGGAALVMWMGELITERGIGNGMSLLIFVGIAARIPAEGQSILESRGGVVFTAVCAAALIIIVGVVFVEQGQRRIPVQYAKRMVGRRMYGGTSTYLPLKVNQAGVIPVIFASSLIYIPHLITQLIRSGSGVVGNSWWDKFVGTYLSDPSNLVYIGIYFGLIIFFTYFYVSITFNPDERADEMKKFGGFIPGIRPGRPTADYLRYVLSRITLPGSIYLGVIAVLPNLFLQIGAGGTVQNLPFGGTAVLIMIGVGLDTVKQIESQLMQRNYEGFLK

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Length
441 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.611 kDa
Sequence
MLSAFISSLRTVDLRRKILFTLGIVILYRVGAALPSPGVNFPNVQQCIKEASAGEAGQIYSLINLFSGGALLKLTVFAVGVMPYITASIIVQLLTVVIPRFEELRKEGQAGQSKMTQYTRYLAIALAILQATSIVALAANGGLLQGCSLDIIADQSIFTLVVIVLVMTGGAALVMWMGELITERGIGNGMSLLIFVGIAARIPAEGQSILESRGGVVFTAVCAAALIIIVGVVFVEQGQRRIPVQYAKRMVGRRMYGGTSTYLPLKVNQAGVIPVIFASSLIYIPHLITQLIRSGSGVVGNSWWDKFVGTYLSDPSNLVYIGIYFGLIIFFTYFYVSITFNPDERADEMKKFGGFIPGIRPGRPTADYLRYVLSRITLPGSIYLGVIAVLPNLFLQIGAGGTVQNLPFGGTAVLIMIGVGLDTVKQIESQLMQRNYEGFLK

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Length
441 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.611 kDa
Sequence
MLSAFISSLRTVDLRRKILFTLGIVILYRVGAALPSPGVNFPNVQQCIKEASAGEAGQIYSLINLFSGGALLKLTVFAVGVMPYITASIIVQLLTVVIPRFEELRKEGQAGQSKMTQYTRYLAIALAILQATSIVALAANGGLLQGCSLDIIADQSIFTLVVIVLVMTGGAALVMWMGELITERGIGNGMSLLIFVGIAARIPAEGQSILESRGGVVFTAVCAAALIIIVGVVFVEQGQRRIPVQYAKRMVGRRMYGGTSTYLPLKVNQAGVIPVIFASSLIYIPHLITQLIRSGSGVVGNSWWDKFVGTYLSDPSNLVYIGIYFGLIIFFTYFYVSITFNPDERADEMKKFGGFIPGIRPGRPTADYLRYVLSRITLPGSIYLGVIAVLPNLFLQIGAGGTVQNLPFGGTAVLIMIGVGLDTVKQIESQLMQRNYEGFLK

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
Length
441 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
49.96 kDa
Sequence
MIKKKLETKLKNFGNQFSELKQRMYFVIFSLIVFRMGSYIPIPGIDTVALASLLEHHRGTIIEMFNMFSGGALSRASIFALGIMPFISSSIIVQILTLIHPKFIEMKKDGEQGRHRINKYIRYITLILAALQSFGMSISLPNIPGLKDVIIDPSISFYGIAIISLITGTIFLMWLGELITEKGIGNGISIIIFSGIVSGLPSSFLNTVEKVRQGSLHVLLFCFIGIVIFLVTLLVVYIERSQRKITISYAKRNLGHRTYSMNSTHLPLKLNMSGVIPAIFASSIVLFPATIASWFGNRDHFKWLVDIVFYLQPTKPLYILTYITAIIFFCFFYTGLAFNPRETADNLKKSGAFILGIRPGEKTAQYINKIMLRLTFLGSMYMAFICLVPELMRFFMDVPFYFGGTSLLIIVVVIIDFISQVQTYIMSTQYESVLKKNKFRF

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Length
441 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
48.29 kDa
Sequence
MAKQPGYQARSTNSGKGELKSRLLFVLGALIVYRIGSFIPVPGIDAAVLAQLVEQQKGTIIDMFNMFSGGALSRASILALGIMPYISASIVIQLLATVSPALAELKKEGAAGQRKISKYTRYATVVFATIQAVAISTGLPNMLSGLVPNVGFSFYFTSVVSLVTGTMFLMWLGEQITERGIGNGISILVFGGIVAGLPSAILQTIEQARQGQMHPLVLLLIAAIVFAVTYFVVFVERGQRRIRVEYAKRQQGRQILGGHSTHLPLKVNMANVMPAIFASSIILFPATLTQWFGQNDKFEWLNNLSMLLNPGQPLYLLVYAVAIIFFSFFYTAMQYNPRDTADNLKKSGAFIPGIRPGEQTSRYIDKVMTRLTLIGGLYVTFVCLVPYIMTSAWDVKFYFGGTSLLIVVVVIMDFIVQVQSHLMSSQYESALKKANLKGFGQ

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Length
440 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.903 kDa
Sequence
MSAIIQAFKDADLRKKIFFTIAMIVLYRIGAQIPSPGVDYATISGRLRDLTQDQSSVYSLINLFSGGALLQLSIFAIGIMPYITASIIVQLLTVVIPHFEELKKEGQSGQAKMMQYTRYLTVALALLQSSGIVALADREQLLGAGIRVLSADRNFFDLIVLVITMTAGAVLVMWMGELITEKGVGNGMSLLIFAGIATRLPTDGMNILGNSGGVVFAVVLASVLILVIGVVFVEQGQRRIPVQYAKRMVGRRQYGGSSTYLPLKVNQAGVIPVIFASSLIYMPVLITQIVNSGSLEVSDNWWQRNIIAHLQTPSSWQYIVLYFALTIFFSYFYVSVQYDPAEQAENMKKYGGFIPGIRPGRPTAEYLGFVMNRLLFVGSLYLAVIAVLPNIMLDLGVDAGSAGATPFGGTAILILVSVALTTVKQIESQLLQSNYEGLLK

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Length
439 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
49.439 kDa
Sequence
MIKKLGLNFKNTKKVTNELKQRIASVVIALIIFRIGSFIPIPGIDTTILSRILNDQKGTIIEMFNMFSGGALSRASIFALGIMPYISSSIIIQLLTLVIPSLSEIKKEGEVGRTKINQYTRYTTLVLALFQSIGIVTSLPKISGMNQIIIHPDFYFYFTAIIILVTGTMFLMWLGELITECGIGNGISIIIFIGIIAGLPSAIVHTIEQTRQGDLHILLFLCVLILIFSVVFLVVFIERSQRKIIIHYAQRQKGRRIYSTQSTHLPLKINMAGVIPAIFASSVVLFPVTIISWFGIDRKCYLLKTIFFYFQPNQPLYLILYVFSIIFFCFFYTGLVFNPRETADNLKKSGGFISGIRPGEQTAKYINKIMIRLTLFGSLYIAFICLIPEFMRSAMNVPFYFGGTSLLIVVVVIMDFIAQIQTLIMSSQYESVLKKANLN

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Lactococcus lactis subsp. lactis (strain IL1403)
Length
439 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
48.455 kDa
Sequence
MFFKTLKEAFKVKDVRARILFTIFILFVFRLGAHITVPGVNVQNLTEVSNLPFLNMMNLVSGNAMQNYSLFAMGVSPYITASIIVQLLQMDILPKFVEWSKQGEIGRRKLNQATRYITLVLAMAQSIGITAGFQAMSSLNIVQNPNWQSYLMIGAILTTGSMVVTWMGEQINEKGFGSGVSVIIFAGIVSSIPSAVKSVYDEKFLNVRPSEIPMSWLFVIGLVLSAIIIIYVTTFVQQAERKVPIQYTKLTQGAPTSSYLPLRVNPAGVIPVIFAGSITTAPATILQFLQRSQGSNVGWLSTLQDALSYTTWTGMLFYALLIVLFTFFYSFVQVNPEKMAENLQKQGSYIPSVRPGKGTEKYVSRLLMRLATVGALFLGLISIIPIAAQNVWGLPKIVALGGTSLLILIQVAIQAVKQLEGYLLKRKYAGFMDNPLETK

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Lactococcus lactis subsp. cremoris
Length
439 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
48.438 kDa
Sequence
MFFKTLKEAFKVKDVRARILFTIFILFVFRLGAHITAPGVNVQNLQQVADLPFLSMMNLVSGNAMQNYSLFAMGVSPYITASIIVQLLQMDILPKFVEWSKQGEIGRRKLNQATRYITLVLAMAQSIGITAGFQAMSSLNIVQNPNWQSYLMIGVLLTTGSMVVTWMGEQINEKGFGSGVSVIIFAGIVSGIPSAIKSVYDEKFLNVRPSEIPMSWIFVIGLILSAIVIIYVTTFVQQAERKVPIQYTKLTQGAPTSSYLPLRVNPAGVIPVIFAGSITTAPATILQFLQRSQGSNVGWLSTLQNALSYTTWTGMLFYALLIVLFTFFYSFVQVNPEKMAENLQKQGSYIPSVRPGKGTEKYVSRLLMRLATVGSLFLGLISIIPIAAQNVWGLPKIVALGGTSLLILIQVAIQAVKQLEGYLLKRKYAGFMDNPLETK

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Synechococcus elongatus (strain PCC 7942)
Length
439 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.151 kDa
Sequence
MVVSRGKTPNAQETFLQMAQASGLRGRILITVGLLILCRLGIFIPVPGIDRVAFSNDLQGNANLGGVIGFLDIFSGGGLSALGVFALGILPYINASIILQLLTAAVPALEDLQKNEGEAGRRKIAQLTRYVSLGWALLQSIVIAVWVTRYAVTPGPLFTIQTALALVAGSMFVMWISELITERGIGNGASLLIFLNIVATLPRSLQQTLELAQSGDRSTVGGIVILLIVFLATIVGIVFVQEGTRRIPVVSARRQVGNRVYSERSSYLPLRLNQGGVMPIIFASAILVLPFSLANFTSNEVVLRIANYLSPNGPTPWIYALFYLVLIVAFSYFYSSLILNPVDLAQNLKKMGSSIPGVRPGRATSQYVQGVLNRLTILGAVFLGLVAIIPTAVEGATRIRTFQGFGATSLLILVGVAIDTAKQVQTYVISQRYEGMVKD

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
Length
439 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.151 kDa
Sequence
MVVSRGKTPNAQETFLQMAQASGLRGRILITVGLLILCRLGIFIPVPGIDRVAFSNDLQGNANLGGVIGFLDIFSGGGLSALGVFALGILPYINASIILQLLTAAVPALEDLQKNEGEAGRRKIAQLTRYVSLGWALLQSIVIAVWVTRYAVTPGPLFTIQTALALVAGSMFVMWISELITERGIGNGASLLIFLNIVATLPRSLQQTLELAQSGDRSTVGGIVILLIVFLATIVGIVFVQEGTRRIPVVSARRQVGNRVYSERSSYLPLRLNQGGVMPIIFASAILVLPFSLANFTSNEVVLRIANYLSPNGPTPWIYALFYLVLIVAFSYFYSSLILNPVDLAQNLKKMGSSIPGVRPGRATSQYVQGVLNRLTILGAVFLGLVAIIPTAVEGATRIRTFQGFGATSLLILVGVAIDTAKQVQTYVISQRYEGMVKD

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Methanococcus vannielii
Length
438 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.615 kDa
Sequence
MKIKPILELIPEVKRPLKGVSFKEKIQWTGLVLILYFILGTIDIYMGGAEMPAMFAFWQTVTASKMGTLITLGIGPIVTAGIIMQLLVGSELISLDLSKPMNRALFQGLQKLFGIFLCFLEAVMFVGAGAFGVVNSTLALILVLQLALGAILVIYLDEIVSRYGIGSGIGLFIAAGVAQTIFVGAFGAEGYLWKFFSAMSVGSLGIAFEYILPILSTLFVFLVVVYVESIRVEIPLAHGRVKGAVGKYPIKFIYVSNLPVILAAALFANIQLWGMFLDRMGYPILGQYSNGTAVSGIAYYFSTPYGISNIISDPLHAIFYTLMMVIFCILFGLFWVETSGLDAKSMAKKLGNLDMAIKGFRKSQKSIEQRLKRYIKPITVMGSAFVGFLAAAADFTGALGGGTGVLLTVSIVYRLYEQLVQEQLSELHPAVAKFVGKR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Mycobacterium leprae (strain TN)
Length
438 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.518 kDa
Sequence
MLSAFISSLRTVDLRRKILFTLGILVLYRVSAALPSPGVNYRHVQQCIQEATAGEAGEIYSLINLFSGGALLKLTVGVMPYITASIIVQLLTVVIPRFEELRKEGQAGQAKMTQYTRYLAIALAVLQATSIVALAANGGLLQGCQEDIISDQSIFSLVVIVLVMTGGAALVMWMGELITERGIGNGMSLLIFVGIAARIPAEGKQILDSRGGVIFAAVCLAALVIIVGVVFVEQGQRRIPVQYAKRMVGRRMYGGTSTYLPLKVNQAGVIPVIFASSLIYIPHLITQLVRSGSGGVGKSWWDKFVGTYLSDPADPVYINIYFGLIIFFTYFYVSVTFNPDERADEMKKFGGFIPGIRPGRPTADYLRYVLSRITLPGSIYLGAIAVLPNLFLQIGNGGEVQNLPFGGTAVLIMIGVGLDTVKQIESQLMQRNYEGFLK

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Length
438 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
48.204 kDa
Sequence
MLKAFWSALQIPELRQRVLFTLLVLAAYRLGAFIPTPGVDLDKIQEFLRTAQGGVFGIINLFSGGNFERFSIFALGIMPYITAAIIMQILVTVVPALEKLSKEGEEGRRIINQYTRIGGIALGAFQGFFLATAFLGAEGGRFLLPGWSPGPFFWFVVVVTQVAGIALLLWMAERITEYGIGNGTSLIIFAGIVVEWLPQILRTIGLIRTGEVNLVAFLFFLAFIVLAFAGMAAVQQAERRIPVQYARKVVGRRVYGGQATYIPIKLNAAGVIPIIFAAAILQIPIFLAAPFQDNPVLQGIANFFNPTRPSGLFIEVLLVILFTYVYTAVQFDPKRIAESLREYGGFIPGIRPGEPTVKFLEHIVSRLTLWGALFLGLVTLLPQIIQNLTGIHSIAFSGIGLLIVVGVALDTLRQVESQLMLRSYEGFLSRGRLRGRNR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS)
Length
437 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
49.14 kDa
Sequence
MVKKLGLNFKNTKTSVSELKQRIVFLIVAIIVFRIGSFIPIPGIDTTILSKILNNQNGTIVDMFNMFSGGALSRASIFALGIMPYISASIIIQLLTLVYPTLSEIKKEGESGRHRINQYTRYATLILALVQSIGIAMTLPNIAGIRSIIINTDFYFYLIAIISLVTSTMFLMWLGELITEYGIGNGISIIIFIGIIAGLPSAIGNTIEKTRQGDLHILLFLFILLLIFSVIFLVVFMERGQRKIVVHYAQRQQGRRIYETPSTHLPLKINMAGVIPAIFASSIVLFPATIISWCKVNHEWLTKILFYLQPNQFLYLILYISAIVFFCFFYTGLVFNPRETADNLKKSGAFISGIRPGEQTAKYINKIMLRLTLVGSLYITFICLIPEFMRSAMNVPFYFGGTSLLIVVVVIIDFITQIQTLIMSNQYESMLKKANLN

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Length
437 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.371 kDa
Sequence
MLTAFARAFKTPDLRKKLLFTLGIIVVYRLGTHIPIPGVDYKNVQECVDQASGNQGLFGLVNMFSGGALLQITVFALGIMPYITASIILQLLTVVIPRLEALKKEGQAGTAKITQYTRYLTVALAILQGTGLVATARSGALFSGCTVAGQIVPDQAIFTTVVMVICMTAGTCVVMWLGELITDRGIGNGMSILMFISIAATFPSALWAIKKQGELADGWIEFGTVILVGLVMVGLVVFVEQAQRRIPVQYAKRMIGRRSYGGTSTYIPLKVNQAGVIPVIFASSLLYIPALIVQFSNSTAGWATWITKNLADTAATPHIILYFFLIVFFAFFYVAISFNPEEVADNMKKYGGFIPGIRAGRPTAEYLSYVLNRITWPGSLYLGLIALVPTMALAGFGANQNFPFGGTSILIIVGVGLETVKQIESQLQQRNYEGFLR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Streptomyces galbus
Length
437 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.496 kDa
Sequence
MLTAFARAFRTPDLRKKLLFTLAIIVVYRVGTHIPIPGVDYKNVQQCVREASGNQGLFGLVNMFSGGALLQITIFALGIMPYITASIILQLLTVVIPRLEALKKEGQAGTAKITQYTRYLTVALAILQGTGLVATARSAPLFGRCSVGGQIVPDQSIFTTITMVICMTAGTCVVMWLGELITDRGIGNGMSILMFISIAATFPSALWAIKKQGTLAGGWIEFGTVIAVGLIMVALVVFVEQAQRRIPVQYAKRMIGRRSYGGTSTYIPLKVNQAGVIPVIFASSLLYIPALVAQFAGGNSGWKSWVEQNLTKGDHPIYIVTYFLLIVFFAFFYVAISFNPEEVADNMKKYGGFIPGIRAGRPTAEYLSYVLNRITWPGSLYLGLIALVPTMALVGFGASQNFPFGGTSILIIVGVGLETVKQIESQLQQRNYEGFLR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Streptomyces griseus
Length
437 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.491 kDa
Sequence
MFTAFARAFKTPDLRKKLLFTLGIIVIYRLGAHIPAPGVDYSKVQQCIDQADSGGLLGLMQMFSGGALLQITIFALGIMPYITASIILQLLTVVIPRLEALKKEGQSGTAKITQYTRYLTVALAILQGTGLVATARSGALFQNCSVGSQIVADKSIFTTIIMVLTMTAGTPPVMWLGELITDRGIGNGMSIPMFISIAATFPGALWAIKESGKLADGWIEFGTVILIGFVMVALVVFVEQAQRRIPVQLPKRMIGRRSYGGTSTYIPLKVNQAGVIPVIFASSLLYIPALIVQFSNSQAGWATWIQDNFVTGDHPYYIATYFVLIVFFAFFYVAISFNPDEVADNMKKYGGFIPGIRAGRPTAEYLSYVLNRITWPGSLYLGLIALVPTMALAGFGGANQNFPFGGTSILIIVGVGLETVKQIESQLQQRNYEGFLR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Streptomyces lividans
Length
437 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.312 kDa
Sequence
MLTAFAPAFKTPDLRKKLLFTLGIIVVYRLGTHIPIPGVDYKNVQECVDQASGNQGLFGLVNMFSGGALLQITVFALGIMPYITASIILQLLTVVIPRLEALKKEGQAGTAKITQYTRYLTVALAILQGTGLVATARSGALFSGCTVAGQIVPDQAIFTTVVMVICMTAGTCVVMWLGELITDRGIGNGMSILMFISIAATFPSALWAIKKQGELADGWIEFGTVILVGLVMVGLVVFVEQAQRRIPVQYAKRMIGRRSYGGTSTYIPLKVNQAGVIPVIFASSLLYIPALIVQFSNSTAGWATWITKNLADTAATPHIILYFFLIVFFAFFYVAISFNPEEVADNMKKYGGFIPGIRAGRPTAEYLSYVLNRITWPGSLYLGLIALVPTMALAGFGANQNFPFGGTSILIIVGVGLETVKQIESQLQQRNYEGFLR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Streptomyces scabiei
Length
437 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.352 kDa
Sequence
MLTAFARAFKTPDLRKKLLFTLGIIVIYRIGTHIPIPGVDYSAVQFCIDQTKSNSGLFGLVNMFSGGALLQITIFALGIMPYITASIILQLLTVVIPRLEALKKEGQSGTAKITQYTRYLTVALAVLQGTGLVATARSGALFSQCPQANNIVPDDSIFTTLTMVVTMTAGTAVVMWLGELITDRGIGNGMSILMFISIAATFPSALWSIKEQGDLAGGWIEFGIVIAVGLVMVALVVFVEQAQRRIPVQYAKRMIGRRSYGGTSTYIPLKVNQAGIIPVIFASSLLYIPALVVQFSGSTAGWAAWIQKNLADTAAPAHITVYFFLIIFFAFFYVAISFNPEEVADNMKKYGGFIPGIRAGRPTAEYLSYVLNRITWPGSLYLGLIALVPTMALAPLGANQNFPFGGTSILIIVGVGLETVKQIESQLQQRNYEGFLR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Length
436 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.444 kDa
Sequence
MKKLIPILEKIPEVELPVKEITFKEKLKWTGIVLVLYFIMGCIDVYTAGAQIPAIFEFWQTITASRIGTLITLGIGPIVTAGIIMQLLVGSGIIQMDLSIPENRALFQGCQKLLSIIMCFVEAVLFVGAGAFGILTPLLAFLVIIQIAFGSIILIYLDEIVSKYGIGSGIGLFIAAGVSQTIFVGALGPEGYLWKFLNSLIQGVPNIEYIAPIIGTIIVFLMVVYAECMRVEIPLAHGRIKGAVGKYPIKFVYVSNIPVILAAALFANIQLWGLALYRMGIPILGHYEGGRAVDGIAYYLSTPYGLSSVISDPIHAIVYMIAMIITCVMFGIFWVETTGLDPKSMAKRIGSLGMAIKGFRKSEKAIEHRLKRYIPPLTVMSSAFVGFLATIANFIGALGGGTGVLLTVSIVYRMYEQLLREKVSELHPAIAKLLNK

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Micrococcus luteus
Length
436 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.324 kDa
Sequence
MLKAIARIVRTPDLLRKIAFTLGLIAVYRMGDFVPATGVDYPAVQQCLAAGNAQGGLYSFVNMFSGGALLQVSVFALGIMPYITASIIVQLLRVVIPRFEQLHQERRRGQATLTQYTRYLTLALALLQATTMASLARTGALLGCSLPLLRDGSILTVLLVVIALTTGCLIVMWFGERITENGVGNGMSLLIFTSIAAGFPAGLGQVVQTQGWRVFAIVMGIGLLTMLAIVFVEESQRRIPVQYAKRQIGSRTVGGSSTYIPVKVNMANVIPVIFASSVLMLPGILIQFNTPQDGSAPAPWITWLSRYFGSGDHPVYMALYFLLIIGFTYFYVSITFNPVEISDNMKRYGGFIPASAPAGPTERYLQYVISRITFVVGALYLGIVAMIPLIAFAVIGTSQNFPLGGTSILIMVGVGLQTVKQVSAQMEQRHYEGLLR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288)
Length
436 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.344 kDa
Sequence
MFFKLLKDAFKIKQVRSKILFTIFIILVFRIGTTITVPGVNAKSLEALSGLSFLNMLSLVSGNAMKNFSVFALGVSPYITASIVVQLLQMDLLPKFVEWGKQGEVGRRKLNQATRYISLALAFVQSIGITAGFNALSSTKLVAAPNWQTYLFIGAVLTTGSMIVVWLGEQITDKGYGNGVSMIIFAGIVASIPEMVKGIYEDYFVNVPSDRLQSSIIFVACLIVAVLLIVYFTTYVQQAEYKIPIQYTKIAQGAPSSSYLPLKVNPAGVIPVIFASSITAAPAAVLQFLSASGNDWGWVRTAQSLLATTTPTGIAMYALLIILFTFFYTFVQINPEKAAENLQKSGAYIPGVRPGKGTEQFMSKLLRRLATVGSLFLGFISIIPIIAKDLFGLSDTVALGGTSLLIIIATGIEGMKQLEGYLLKRKYTGFMNTTTK

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Vaucheria litorea
Length
436 amino acids
Function
The central subunit of the protein translocation channel SecYE. Consists of two halves. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug (By similarity).
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
49.694 kDa
Sequence
MNTKLQDSKSPRLKNRILLTISLLTIVRIGSFIPVPYITKEVLVNLLSAENSSNNTFAQLLNTFSGGGNSSFGLLSLGILPYINASIIIQLLTTIIPALSKMQKDEGEYGRRKLVDFTRYLTFFWAIVESISISYSLREVIFEWNLQVYFLISLSLITGSMIVLWFSELITKNGLGNGSSLLICFNIVSNLPDQIKFSLISLKNQINNFSNIFLLISIFLITTIGCIYINEAIIKIPLVSARQLLKKTKSEEKNSSNSILPLRINQAGVMPLVFTSYAILFFSSLFEIIKKQTNIFNIFFQYPILNSVISYWFLKILFWIFYATLIFFFTYFYSTIVLDPKDVAERFRKNSVVILGISPGSSTRSYLSKILRFIAKINAIFLIYNIIGLQILESILNLNIINIRGLGFTSQLILVNVLIDTIKRIRSFLNEEENYF

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Streptococcus sanguinis (strain SK36)
Length
435 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.469 kDa
Sequence
MFFKLLKDAFKIKQVRSKILFTIFIILVFRIGTTITVPGINAKALSNLNDLPFLNMLSLVSGNAMRNFSVFALGVSPYITASIVVQLLQMDLLPKFVEWGKQGEVGRRKLNQATRYIALVLAFVQAIGITAGFDTLSRANLVANPNVQTYALICVLLATGSMIVTWLGEQITDKGYGNGVSMIIFAGIVSAIPDMIKGIYEDYFVNIPSERLTSSFIFVGILIVAVLLIIYFTTFVQQAEYKIPIQYTKVAKGAPSSSYLPLKVNPAGVIPVIFASSITAAPAAIFQVVSALGYDADWVKTAQSLLATTTISGMFMYAFLIVLFTFFYTFVQINPEKTAENLQKSGAYIPGVRPGKGTEDYMSKLLRRLATVGSLFLGFISILPILAKDVFGLTDAVALGGTSLLIIISTGIEGMKQLEGYLLKRKYVGFMDTSE

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Length
434 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
48.61 kDa
Sequence
MKELFLSLFTVKDLRNKFLFTLFVLFLFRVGSYLPIPGIDSVALKSYFKSQSDFSIANYFDFFSGGAFSNFSIFMLSIGPYISASIIVQLLVYSFPSLKKMQEGDGGRQKTKKYTKYLTIVAAVVQGYATSLYAKGIPGAVTIPFYRYIFVAILTVTTGTFILLWFGEQINQRGVGNGTSLIIFSGIVVRLQAALFNLFQSMQDPSQNVNPVFVILIISIFILVVILIIYEYKAQMRIAIHYARANSNNTVSSYLPIKLNPSGVLPVIFASVLITLPLQILSGFAETSSIARQILSYLRPNGFYYTFLNVILIIGFTYFYSKIQLSPKDISNNIRKNGGTIPGIKSDEMEKYLDEIMNKTLFSGSIFLSIIAIIPFLVQNIFRFPHDVSRIMGGSSLLIMVGVALDTLIHIDAYLKTQGFSHGNKKNYAFLQKI

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Rickettsia bellii (strain RML369-C)
Length
433 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.47 kDa
Sequence
MNQNFSKKSSNDLINRIIFTIFVLIICRFGSFIPIAGIDAIALGSIAEKNQSGILGMFNMLSGGSLGRMSIFALAIMPYITASIIIQLMSVAYKPLENLKKEGEAGKRKINQLSRYLTVLLASLQAYGVAVSLESIVTNTGPVVIIPGLFFKITTVITLVVGTMLLMWLGEQITQRGIGNGTSLIIFIGIISGVPSAIISMFELSRKGALSPLVAIAVCAGVVILISIIIFFEKAQRKLLVQYPKRQVGNKIYGGDSTYMPLKLNTSGVIPPIFASSILLFPATLANFSSSNSEIMNMLTYYLGHGKPIYILLYVALIMFFSFFYTAIVFNSEETANNLRKYGAYIPGKRPGKNTSEYFDYILTRLTVVGGIYLSVICIIPELLMNKYVISLSLGGTSFLIVVNVVLDTLTQIQTYLFSSKYESLMKKVKLKN

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Rickettsia conorii (strain ATCC VR-613 / Malish 7)
Length
433 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.335 kDa
Sequence
MGQNFSKKSGNDLVSRIVFTILILIVCRFGSFIPIPGIDSIALSSVAAQNQSGILGMFNMLSGGSLGRMSIFALAIMPYITASIIIQLMSVAYKPLENLKKEGEVGKRKVNQLSRYLTVLLASFQAYGVAISLESIVTNTGPVVILAGFFFRITTVITLVVGTMLLMWLGEQITQRGIGNGTSLIIFIGIISGVPSAIISMFELSRKGALSPLIAIAVCIGVVVLIAIIIFFERAQRKLLVQYPKRQVGNKIYGGEATHMPLKLNTSGVIPPIFASSILLFPATLANFSNSNSETMGMLTYYLGHGKPVYILLYVALIMFFSFFYTAIVFNSEETANNLRKYGAYIPGKRPGKNTSDYFDYILTRLTVIGGIYLSVICVIPELLMNKYVISLSLGGTSFLIVVNVVLDTMTQIQTYLFSSKYEGLMKKVKLKN

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Rickettsia felis (strain ATCC VR-1525 / URRWXCal2)
Length
433 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.351 kDa
Sequence
MGQNFSKKSGNDLVSRIVFTILILIVCRFGSFIPIPGIDSIALSSVAEKNQSGILGMFNMLSGGSLGRMSIFALAIMPYITASIIIQLMSVAYKPLENLKKEGEVGKRKVNQLSRYLTVLLASFQAYGVAISLESIVTNTGPVVILAGFFFRVTTVITLVVGTMLLMWLGEQITQRGIGNGTSLIIFIGIISGVPSAIISMFELSRKGALSPLIALAVCIGVVVLIAIIIFFEKAQRKLLVQYPKRQVGNKIYGGEATHMPLKLNTSGVIPPIFASSILLFPATLANFSNSNSETMGMLTYYLGHGKPVYILLYVALIMFFSFFYTAIVFNSEETANNLRKYGAYIPGKRPGKNTSDYFDYILTRLTVIGGIYLSVICVIPELLMNKYVISLSLGGTSFLIVVNVVLDTMTQIQTYLFSSKYEGLMKKVKLKN

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Rickettsia prowazekii (strain Madrid E)
Length
433 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.697 kDa
Sequence
MGQNFSKKSSNDLVNRIIFTLFMLIICRFGSFIPIPGIDSIALNSVAEKNQFGILGMFNMLSGGSLGRMSIFALAIMPYITASIIIQLMSVAYKPLENLKKEGETGKRKINQLSRYLTVLLASFQAYGVALSLESMVTNTGPVVILAGFFFRVTTVITLVVGTILLMWLGEQITQRGIGNGTSLIIFIGIISGVPSAIISMFELSRKGALSPLIAITVCIGVVLLIAIIIFFEKAQRKLLVQYPKRQVGNKIYGGEATHMPLKLNTSGVIPPIFASSILLFPTTLASFSNSNSDTMSMLTYYLGHGKPVYILLYVVLIMFFSFFYTAIVFNSEETANNLRKYGAYIPGKRPGKNTSDYFDYILTRLTVIGGIYLSVICVIPELLMNKYVISLSLGGTSFLIVVNVVLDTMTQIQTYLFSSKYEGLMKKIKLKN

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Rickettsia typhi (strain ATCC VR-144 / Wilmington)
Length
433 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.681 kDa
Sequence
MGQNFSKKSSNDLVSRIIFTIFMLIICRIGSFIPIPGIDSIALNSVAEKNQFGILGMFNMLSGGSLGRMSIFALAIMPYITASIIIQLMSVAYKPLENLKKEGESGKRKINQLSRYLTVLLASFQAYGVALSLESMVTNTGPVVILAGFFFRVTTVITLVVGTMLLMWLGEQITQRGIGNGTSLIIFIGIISGVPSAIISMFELSRKGALSPLIAITVCIGVVLLIAIIIFFEKAQRKLLVQYPKRQVGNKIYGGEATHMPLKLNTSGVIPPIFASSILLFPTTLANFSNSNSETMSMLSYYLGHGKPVYILLYVVLIMFFSFFYTAIVFNSEETANNLRKYGAYIPGKRPGKNTSDYFDYILTRLTVIGGLYLSIICVIPELLMNKYVISLSLGGTSFLIVVNVVLDTMTQIQTYLFSSKYEGLMKKIKLKN

Gene
secY
Protein
Protein translocase subunit SecY 1
Organism
Lactobacillus kefiranofaciens (strain ZW3)
Length
431 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.691 kDa
Sequence
MFSTLKNAFKDKEIRNKIYFTLFILLLYRIGANITVPGINVKAITQVAQTGLVPMLDTVSGGGLDNYSIFSLGVSPYITAQIVIQLLQMDIVPTLVEWGKQGEVGRRKTNQVTRYLTLVVAFVQSIGITLGFNALTQMGLVKNQTPQTYVEIAIIMTAGTMLLTWLGDEITDKGLGNGVSVIIFAGIIARLPSGLYQIYKEEIINNSASDRWQGILFFIAVIVAILIVTQLVTWVEQADRRIPIQYTRRATISGSESFLPLKVNVSGVIPVIFASSFIVTPATILMAFQRTQGDQQWFKVMNQIFSLQTTPGVIIYTLLIILFTFFYAFVQVNPEKLAENLQKQGAYIPSVWPGKDTQDYVSKMLIKLSTVGSIFLGLVALLPQLATNFWNLPSSIGLGGTSLLIVIGVVLELSRQINGLLMKREYVGFIR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46)
Length
431 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.03 kDa
Sequence
MFKTISNFMRVKDIRNKIIFTLLMLIVFRLGSFIPVPHVNTEVLKAQDQMSVFGILNTFGGGALFNFSILAMGIMPYITASIIIQLLQMDVVPKFTEWSKQGEVGRRKLAQFTRYFTIVLGFIQALGMSYGFNNMAGGALITDPGVGTYLLIAIVLTAGTAFLMWLGEQITSHGVGNGISIIIFAGIVAGIPQTINQIYAQQFVDAGDQLFLQIIKVVVILVAILAIVVGVIFIQQAVRKISIQYAKGSGRSPVPGGQSTHLPLKVNPAGVIPVIFAVAFITTPRTVATFFGSNDVTNWIQKTFDYTHPVGMGVYAALIIAFTYFYAFVQVNPEQMADNLKKQGGYIPGVRPGKMTQDRITSILYRLTFVGSIFLAVIAILPVLFVNIAGLPSSAQIGGTSLLIVIGVALETMKQLESQLVKRNYRGFMKH

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Bacillus subtilis (strain 168)
Length
431 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.243 kDa
Sequence
MFKTISNFMRVSDIRNKIIFTLLMLIVFRIGAFIPVPYVNAEALQAQSQMGVFDLLNTFGGGALYQFSIFAMGITPYITASIIIQLLQMDVVPKFTEWSKQGEVGRRKLAQFTRYFTIVLGFIQALGMSYGFNNLANGMLIEKSGVSTYLIIALVLTGGTAFLMWLGEQITSHGVGNGISIIIFAGIVSSIPKTIGQIYETQFVGSNDQLFIHIVKVALLVIAILAVIVGVIFIQQAVRKIAIQYAKGTGRSPAGGGQSTHLPLKVNPAGVIPVIFAVAFLITPRTIASFFGTNDVTKWIQNNFDNTHPVGMAIYVALIIAFTYFYAFVQVNPEQMADNLKKQGGYIPGVRPGKMTQDRITSILYRLTFVGSIFLAVISILPIFFIQFAGLPQSAQIGGTSLLIVVGVALETMKQLESQLVKRNYRGFMKN

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Length
431 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
48.17 kDa
Sequence
MWQAFKNAFKIPELRDRIIFTFLALIVFRMGIYIPVPGLNLEAWGEIFRRIAETAGVAGILSFYDVFTGGALSRFSVFTMSVTPYITASIILQLLASVMPSLKEMLREGEEGRKKFAKYTRRLTLLIGGFQAFFVSFSLARSNPDMVAPGVNVLQFTVLSTMSMLAGTMFLLWLGERITEKGIGNGISILIFAGIVARYPSYIRQAYLGGLNLLEWIFLIAVALITIFGIILVQQAERRITIQYARRVTGRRVYGGASTYLPIKVNQGGVIPIIFASAIVSIPSAIASITNNETLKNLFRAGGFLYLLIYGLLVFFFTYFYSVVIFDPREISENIRKYGGYIPGLRPGRSTEQYLHRVLNRVTFIGAVFLVVIALLPYLVQGAIKVNVWIGGTSALIAVGVALDIIQQMETHMVMRHYEGFIKKGKIRGRR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Length
430 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
46.91 kDa
Sequence
MFRTISNIFRVGDLRRKVIFTLLMLIVFRIGSFIPVPGTNREVLDFVDQANAFGFLNTFGGGALGNFSIFAMGIMPYITASIVMQLLQMDVVPKFAEWAKEGEAGRRKLAQFTRYGTIVLGFIQALGMSVGFNNFFPGLIPNPSVSVYLFIALVLTAGTAFLMWLGEQITAKGVGNGISIIIFAGIAAGIPNGLNLIYSTRIQDAGEQLFLNIVVILLLALAILAIIVGVIFVQQALRKIPVQYAKRLVGRNPVGGQSTHLPLKVNAAGVIPVIFALSLFIFPPTVAGLFGSDHPVAAWVIETFDYTHPIGMAVYALLIIGFTYFYTFIQVNPERMAENLKKQGGYIPGIRPGKATQTYITRILYRLTFVGSLFLAVVAILPVFFIKFADLPQAIQIGGTGLLIVVGVALDTMKQIEAQLIKRSYKGFIK

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Staphylococcus aureus (strain NCTC 8325)
Length
430 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.148 kDa
Sequence
MIQTLVNFFRTKEVRNKIFFTLAMLVIFKIGTYIPAPGVNPAAFDNPQGSQGATELLNTFGGGALKRFSIFAMGIVPYITASIVMQLLQMDIVPKFSEWAKQGEVGRRKLNNVTRYLAISLAFIQSIGMAFQFNNYLKGALIINQSIMSYLLIALVLTAGTAFLIWLGDQITQFGVGNGISIIIFAGILSTLPASLIQFGQTAFVGQEDTSLAWLKVLGLLVSLILLTVGAIYVLEAVRKIPIQYAKKQTAQRLGSQATYLPLKVNSAGVIPVIFAMAFFLLPRTLTLFYPDKEWAQNIANAANPSSNVGMVVYIVLIILFTYFYAFVQVNPEKMADNLKKQGSYVPGIRPGEQTKKYITKVLYRLTFVGSIFLAVISILPILATKFMGLPQSIQIGGTSLLIVIGVAIETMKSLEAQVSQKEYKGFGGR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Staphylococcus aureus (strain COL)
Length
430 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.148 kDa
Sequence
MIQTLVNFFRTKEVRNKIFFTLAMLVIFKIGTYIPAPGVNPAAFDNPQGSQGATELLNTFGGGALKRFSIFAMGIVPYITASIVMQLLQMDIVPKFSEWAKQGEVGRRKLNNVTRYLAISLAFIQSIGMAFQFNNYLKGALIINQSIMSYLLIALVLTAGTAFLIWLGDQITQFGVGNGISIIIFAGILSTLPASLIQFGQTAFVGQEDTSLAWLKVLGLLVSLILLTVGAIYVLEAVRKIPIQYAKKQTAQRLGSQATYLPLKVNSAGVIPVIFAMAFFLLPRTLTLFYPDKEWAQNIANAANPSSNVGMVVYIVLIILFTYFYAFVQVNPEKMADNLKKQGSYVPGIRPGEQTKKYITKVLYRLTFVGSIFLAVISILPILATKFMGLPQSIQIGGTSLLIVIGVAIETMKSLEAQVSQKEYKGFGGR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Length
430 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.148 kDa
Sequence
MIQTLVNFFRTKEVRNKIFFTLAMLVIFKIGTYIPAPGVNPAAFDNPQGSQGATELLNTFGGGALKRFSIFAMGIVPYITASIVMQLLQMDIVPKFSEWAKQGEVGRRKLNNVTRYLAISLAFIQSIGMAFQFNNYLKGALIINQSIMSYLLIALVLTAGTAFLIWLGDQITQFGVGNGISIIIFAGILSTLPASLIQFGQTAFVGQEDTSLAWLKVLGLLVSLILLTVGAIYVLEAVRKIPIQYAKKQTAQRLGSQATYLPLKVNSAGVIPVIFAMAFFLLPRTLTLFYPDKEWAQNIANAANPSSNVGMVVYIVLIILFTYFYAFVQVNPEKMADNLKKQGSYVPGIRPGEQTKKYITKVLYRLTFVGSIFLAVISILPILATKFMGLPQSIQIGGTSLLIVIGVAIETMKSLEAQVSQKEYKGFGGR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Staphylococcus aureus (strain N315)
Length
430 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.148 kDa
Sequence
MIQTLVNFFRTKEVRNKIFFTLAMLVIFKIGTYIPAPGVNPAAFDNPQGSQGATELLNTFGGGALKRFSIFAMGIVPYITASIVMQLLQMDIVPKFSEWAKQGEVGRRKLNNVTRYLAISLAFIQSIGMAFQFNNYLKGALIINQSIMSYLLIALVLTAGTAFLIWLGDQITQFGVGNGISIIIFAGILSTLPASLIQFGQTAFVGQEDTSLAWLKVLGLLVSLILLTVGAIYVLEAVRKIPIQYAKKQTAQRLGSQATYLPLKVNSAGVIPVIFAMAFFLLPRTLTLFYPDKEWAQNIANAANPSSNVGMVVYIVLIILFTYFYAFVQVNPEKMADNLKKQGSYVPGIRPGEQTKKYITKVLYRLTFVGSIFLAVISILPILATKFMGLPQSIQIGGTSLLIVIGVAIETMKSLEAQVSQKEYKGFGGR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Staphylococcus aureus (strain MRSA252)
Length
430 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.148 kDa
Sequence
MIQTLVNFFRTKEVRNKIFFTLAMLVIFKIGTYIPAPGVNPAAFDNPQGSQGATELLNTFGGGALKRFSIFAMGIVPYITASIVMQLLQMDIVPKFSEWAKQGEVGRRKLNNVTRYLAISLAFIQSIGMAFQFNNYLKGALIINQSIMSYLLIALVLTAGTAFLIWLGDQITQFGVGNGISIIIFAGILSTLPASLIQFGQTAFVGQEDTSLAWLKVLGLLVSLILLTVGAIYVLEAVRKIPIQYAKKQTAQRLGSQATYLPLKVNSAGVIPVIFAMAFFLLPRTLTLFYPDKEWAQNIANAANPSSNVGMVVYIVLIILFTYFYAFVQVNPEKMADNLKKQGSYVPGIRPGEQTKKYITKVLYRLTFVGSIFLAVISILPILATKFMGLPQSIQIGGTSLLIVIGVAIETMKSLEAQVSQKEYKGFGGR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Staphylococcus aureus (strain MSSA476)
Length
430 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.148 kDa
Sequence
MIQTLVNFFRTKEVRNKIFFTLAMLVIFKIGTYIPAPGVNPAAFDNPQGSQGATELLNTFGGGALKRFSIFAMGIVPYITASIVMQLLQMDIVPKFSEWAKQGEVGRRKLNNVTRYLAISLAFIQSIGMAFQFNNYLKGALIINQSIMSYLLIALVLTAGTAFLIWLGDQITQFGVGNGISIIIFAGILSTLPASLIQFGQTAFVGQEDTSLAWLKVLGLLVSLILLTVGAIYVLEAVRKIPIQYAKKQTAQRLGSQATYLPLKVNSAGVIPVIFAMAFFLLPRTLTLFYPDKEWAQNIANAANPSSNVGMVVYIVLIILFTYFYAFVQVNPEKMADNLKKQGSYVPGIRPGEQTKKYITKVLYRLTFVGSIFLAVISILPILATKFMGLPQSIQIGGTSLLIVIGVAIETMKSLEAQVSQKEYKGFGGR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Staphylococcus aureus (strain MW2)
Length
430 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.148 kDa
Sequence
MIQTLVNFFRTKEVRNKIFFTLAMLVIFKIGTYIPAPGVNPAAFDNPQGSQGATELLNTFGGGALKRFSIFAMGIVPYITASIVMQLLQMDIVPKFSEWAKQGEVGRRKLNNVTRYLAISLAFIQSIGMAFQFNNYLKGALIINQSIMSYLLIALVLTAGTAFLIWLGDQITQFGVGNGISIIIFAGILSTLPASLIQFGQTAFVGQEDTSLAWLKVLGLLVSLILLTVGAIYVLEAVRKIPIQYAKKQTAQRLGSQATYLPLKVNSAGVIPVIFAMAFFLLPRTLTLFYPDKEWAQNIANAANPSSNVGMVVYIVLIILFTYFYAFVQVNPEKMADNLKKQGSYVPGIRPGEQTKKYITKVLYRLTFVGSIFLAVISILPILATKFMGLPQSIQIGGTSLLIVIGVAIETMKSLEAQVSQKEYKGFGGR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Staphylococcus carnosus (strain TM300)
Length
430 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.386 kDa
Sequence
MFETFVNFFKTKEVRNKIFFTLAMLVIFKIGTYIPAPGVNPAAFDNNQGSQGVTDLLNTFGGGALKNFSIFAMGIMPYITASIVMQLLQMDIVPKFTEWAKQGDVGRKKLNNVTRYFAIILAFIQSIGMAFQFNNYLKGALIIDPSPMSYLLIAIVLTTGTAFLLWLGEQITQYGVGNGISIIIFAGILSTLPSSLIQFYQQAFVGQSDTTMAWLQVAGLVIGLVLLTMGAVYVLQAVRKIPIQYAKKQSTQRLGSNATYLPLKVNSAGVIPVIFAMAFFLLPRTLTMFFPKADWAQQIANTANPSSNIGMVIYIILIIAFTYFYAFVQVNPEKMSDNLKKQGSYVPGIRPGEQTKKYITKVLYRLTFVGSIFLAVIAILPILATKFMNLPQSIQVGGTSLLIVIGVAIETMKSLEAQVNQKEYKGFGGR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Staphylococcus epidermidis (strain ATCC 35984 / RP62A)
Length
430 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.419 kDa
Sequence
MFQTFVRFFTTKEVRNKIFFTLAMLVIFKIGTYIPAPGVNPEAFNHPQGSQGATELLNTFGGGALKRFSIFAMGIMPYITASIVMQLLQMDIVPKFTEWAKQGEMGRRKINNVTRYFAIILAFIQSIGMAFQFNNYLKGQLIIEKSVMSYLLIAVVLTAGTAFLIWLGDQITQFGVGNGISLIIFAGILSTLPSSLEQFAQSVFVGQDDTSLAWLKILGLIVALILLTVGAIFVLEAKRKIPIQYAKKQSAQRLGSQATYLPLKVNSAGVIPVIFAMAFFLLPRTLTLFFPKAEWAQNIADTANPSSNIGMIIYVVLIIAFAYFYAFVQVNPEKMADNLKKQGSYVPGIRPGEQTKKYITKVLYRLTFVGSIFLAAIAILPIIATKFMGLPQSIQIGGTSLLIVIGVAIETMKTLEAQVTQKEYKGFGGR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Staphylococcus epidermidis (strain ATCC 12228)
Length
430 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.419 kDa
Sequence
MFQTFVRFFTTKEVRNKIFFTLAMLVIFKIGTYIPAPGVNPEAFNHPQGSQGATELLNTFGGGALKRFSIFAMGIMPYITASIVMQLLQMDIVPKFTEWAKQGEMGRRKINNVTRYFAIILAFIQSIGMAFQFNNYLKGQLIIEKSVMSYLLIAVVLTAGTAFLIWLGDQITQFGVGNGISLIIFAGILSTLPSSLEQFAQSVFVGQDDTSLAWLKILGLIVALILLTVGAIFVLEAKRKIPIQYAKKQSAQRLGSQATYLPLKVNSAGVIPVIFAMAFFLLPRTLTLFFPKAEWAQNIADTANPSSNIGMIIYVVLIIAFAYFYAFVQVNPEKMADNLKKQGSYVPGIRPGEQTKKYITKVLYRLTFVGSIFLAAIAILPIIATKFMGLPQSIQIGGTSLLIVIGVAIETMKTLEAQVTQKEYKGFGGR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Aquifex aeolicus (strain VF5)
Length
429 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently (By similarity).
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
48.1 kDa
Sequence
MSEYLKALFELKELRQKFIFTLLMFVIYRLGSHIPIPGINPEALRDFLKAFEGSVFALYDIFSGGNLGRLTVFALGVMPYISASIMMQLLTVAIPSLQRLAKEEGDYGRYKINEYTKYLTLFVATVQSLGIAFWIRGQVSPKGIPVVENPGISFILITVLTLVAGTMFLVWIADRITEKGIGNGASLIIFAGIVANFPNAVIQFYEKVKTGDIGPLTLLLIIALIIAIIVGIVYVQEAERRIPIQYPGRQVGRQLYAGRKTYLPIKINPAGVIPIIFAQALLLIPSTLLNFVQNPFIKVIADMFQPGAIFYNFLYVTFIVFFTYFYTAVLINPVELAENLHKAGAFIPGVRPGQDTVKYLERIINRLIFFGALFLSVIALIPILISVWFNIPFYFGGTTALIVVGVALDTFRQIETYLIQKKYKSYVRR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Trieres chinensis
Length
425 amino acids
Function
The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
47.396 kDa
Sequence
MKQTDDKDSLLNRLLLSLGILLFIRMGTFLPVPGIDHGHLEFYIERHFRLRTLVSTFAGDNTVVVGLFTLNIFPYINASIIMQLLVSLLPGLSKLQKEGGAEARRSINSLTRLLTLGWSLIQSTSVAFYLKRALFEWNLVLAFEIVIWLTTGAMIVLWLSEIITEYGLGNGPSLLIYTNIVSSLPGFVKQVITESSGKVPIGSWLLSGFVLFVALYGIVLLQEGMRKVYLISSKQLNQTSLPFSGSSNLESGYYIPLRFNQAGVMPIILTTAVLVIPTFIYNLGLLRILTPLITLPVFVKSYKIIYWVSYFVLILLFSLFYSTIVVNPKDLSDELQKMAVSIPGIRPGVETTFYLKQVMKRVTLLGAIMLALLATLPNIIQAILSLSGFTNLGTTSLLILVGVILDLTREMRSIILSNIYYDMFD

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Emiliania huxleyi
Length
422 amino acids
Function
The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug (By similarity).
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
46.182 kDa
Sequence
MEQSTTRSLLKGKILKILTLLLLVRLGLYIPVPGVELDILTQGQTSNPMFGFAKTLVGNSFLGIGSLGILPYINASIIIQLLTPLFPNLERLQKEEGELGRQQISRYTRYLTCIWAIVLSSAIAFFLIKPITFGWSLKLGLEIVLSLTVGSILSMWFAELITEESLGNGSSMIIFINIVGGIPNNLSSLSKTFSAANLASAIPLLLTGLGIYLGIVLIIIFFQESYKKITIVSAKQLNLTTSAQTQSERLANNSFIPLKLNQGGIMPLVFSSTIAVVFMYPAQILLSSALLTNAAGLASKLLTIYSFGINFVLVIFFSCFYVSLVLKPKDMSENLGKMAYSIPGIRQGKETTKYLEKVINRLAFIGGLFLAFLAFFPLFVGNFIQFGLFKNLTSLLILIGVITDTTSQITGYLVSTRYEGLK

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Helicobacter pylori (strain ATCC 700392 / 26695)
Length
420 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
45.829 kDa
Sequence
MNKAIASKILITLGFLFLYRVLAYIPIPGVDLAAIKAFFDSNSNNALGLFNMFSGNAVSRLSIISLGIMPYITSSIIMELLSATFPNLAKMKKERDGMQKYMQIVRYLTILITLIQAVSVSVGLRSISGGANGAIMIDMQVFMIVSAFSMLTGTMLLMWIGEQITQRGVGNGISLIIFAGIVSGIPSAISGTFNLVNTGVINILMLIGIVLIVLATIFAIIYVELAERRIPISYARKVVMQNQNKRIMNYIPIKLNLSGVIPPIFASALLVFPSTILQQATSNKTLQAVADFLSPQGYAYNILMFLLIIFFAYFYSSIVFNSKDIADNLRRNGGYIPGLRPGEGTSSFLNSVASKLTLWGSLYLALISTVPWILVKAMGVPFYFGGTAVLIVVQVAIDTMKKIEAQIYMSKYKTLSAVGF

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Guillardia theta
Length
420 amino acids
Function
The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug (By similarity).
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
46.937 kDa
Sequence
MNTSIKSIKKQDLKDRIVFTLFLIVMSRLGTFLPIPGVDHDAFYQSIISNPLVNFLNVFSGGGFASIGVFALGIVPYINASIIVQLATNSIPSLEKLQKEEGELGRQKIVQLTRYVALVWALIQSIGVSFWVRPYVFNWDLNFVFAMSLTLTIGSMLIMWFSEQITEKGIGNGPSLLIFINIISGLPKLLQSQIQSTRLNIQALDIFVLVFIFSVMIIGIIFIQEGIKRIPIISARQLGKGQMDNKTSYLPLKLNQSGVMPIIFASAVLVLPAYLAQLVSNEQLRTVLHLFDGTSNNKLLYLLFYFTLILFFSYFYTSLILNPNDVSKNLKKMESSIYGVRPGKATTEYLQKTLNRLTFLGALFLAFIAIVPNIIETLTNLSVFKGLGGTSLLIIVGVQVDTSKQIQTYLISKNYETIVR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Helicobacter pylori (strain J99 / ATCC 700824)
Length
420 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
45.827 kDa
Sequence
MNKAIASKILITLGFLFLYRVLAYIPIPGVDLAAIKAFFDSNSNNALGLFNMFSGNAVSRLSIISLGIMPYITSSIIMELLSATFPNLAKMKKERDGMQKYMQIVRYLTILITLIQAVSVSVGLRSISGGANGAIMIDMQVFMIVSAFSMLTGTMLLMWIGEQITQRGVGNGISLIIFAGIVSGIPSAISGTFNLVNTGVINILMLIGIVLIVLATIFAIIYVELAERRIPISYARKVVMQNQNKRIMNYIPIKLNLSGVIPPIFASALLVFPSTILQQATSNKTLQAIADFLSPQGYAYNILMFLLIIFFAYFYSSIVFNSKDIADNLRRNGGYIPGLRPGEGTSSFLNAVASKLTLWGSLYLALISTVPWILVKAMGVPFYFGGTAVLIVVQVAIDTMKKIEAQIYMSKYKTLSAVGF

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Diacronema lutheri
Length
419 amino acids
Function
The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
46.618 kDa
Sequence
MKKAFVLEGPLVLRLFRTIMILIFARLGNYIPIPGITEVESFYESSFRNTSIYNLSALSGGSNVISILTLGLGPFFSASLAVQFLVKLYPAFEKLQNEEGEEGRKTIVRYTRILTVLFCIIESFFLSNSLRSFVFNWNSISYFVVAAAVTTGSLVLVWLSEVITERGIGNGSSLLILIGNLSRFRFLINKDDFDSLNVSSQSNLYIIYIIITLVSMLIFSTLSQEGARKIPVVSAKQLIDGVEDDMRRSYIPIRFGQAGVVPIIFSSSILLFLTTSIKQLPNANIATRVILDSVNLQQIFYFFTFLVLIIFFSFFYTLIILSPSDIAKNLKKMSSVIQDTKPGVATKVYIRKFILQASFVGSILLSALILIPSILAAALGVHPLSISGITSLILSFSIINDTVRQVLAYRDTRKFLLSS

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Pyrenomonas salina
Length
412 amino acids
Function
The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
45.869 kDa
Fragment
single
Sequence
MESIRRNSRKEGIKERIFLTIGLLVLSRLGTFIPVPGVDHDAFYQSISTNPIVTFLNIFSGGGFASIGIFALGIVPYINASIVIQLATTSIPNLEKLQKEEGEAGRQKISQITRYRALGWAAIQSLGVSFWVRPYVFNWDSQFVVQMTLALTTGSMLIMWFSEQITEKGIGNGPSLLIFINIIAGLPKLIQQKSNAISSTNQTTELVVLASISVYDSRIFIRDRRYYILQTVGRHCKQTSYLPLRLNQGGVMPIIFASAILVLPAYLGQVIQNQFVLKLVTLLSPNSSDKNLYLIFYFSLILFFSYFYASLIINPNDVSQNLKKMESSIPGVRPGKATTDYLQKTLNRLTFLGALFLAFIAVVPSIIENITSISTFKGLGATSLLILVGVAIDTSRQIQTYLISRNYENIMK

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Porphyra purpurea
Length
411 amino acids
Function
The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
45.66 kDa
Sequence
MSQKSDLRNRIKFTLLLLVLARLGIFIPVPGIDHDAFYASVEKNTLVNFLNIFSGGGFSTIGIFALGIVPYINSSIVMQLLTKIIPDLEKLQKEEGELGRQKITQITRYLALGWATLQSGAISIWVKPYVFNWNFTFVCESVLALTAGSMIIMWLSELITEKGIGNGASLLIFQNIVSGLPKNFTQSFFDANYSNTSIKFGLFIVIFLLMIIITIFVQEGTRRIKIISARQLGKSSILDPNSYLPLKLNQGGVMPIVFASASMALPAYLTQLTQNTFLLQVLYLFCPNGSLYLVLYSVLILFFSYFYTSIVMNPEDIATNLKKMGASIPNIRPGQATIDYLQVILNRLTFLGATFLFTVALIPFIIEKVAQIQNLRGLGATSLLILVGVAIDTAKQIQTYVISKKYDSMTK

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Pyropia yezoensis
Length
411 amino acids
Function
The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
45.558 kDa
Sequence
MSQKSDLRNRIIFTLFLLVLARLGIFIPVPGIDHDAFYASVEKNTLVNFLNIFSGGGFSTIGIFALGIVPYINSSIVMQLLTKIVPNLEKLQKEEGELGRQKITQITRYLALGWATLQSGAISIWVKPYVFNWNFAFVCESVLALTAGSMIIMWLSELITEKGIGNGASLLIFQNIVSGLPKNFTQSFFDASYSNASLKFGLFIAIFLLMIIITICVQEGTRRIKIISARQLGKSSILDPNSYLPLKLNQGGVMPIVFASASMALPSYLTQIIQNKTLLQILYLFCPNGSLYLLLYCALILFFSYFYTSIVMNPEDIAINLKKMGASIPNIRPGQATIDYLQVILNRLTFLGASFLFTVALIPFIIEKVTQIQNLRGLGATSLLILVGVAIDTAKQIQTYVISKKYDSMTK

Gene
secY
Protein
Protein translocase subunit SecY 2
Organism
Lactobacillus kefiranofaciens (strain ZW3)
Length
410 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
45.057 kDa
Sequence
MILIIYRALFFVTIPGVNSAALAKLSNNSSLTMLSMFSGGGFENFSIMSLGVTAYITAQIIVQLLQADVIPTFTQWSKEGQTGRKKLDQVTRSLTLVLGLVQATGITLGINTLTNGKFMIENNPFTIIVIAVSMTAGSFIAMWLGDLITENGLGNGISVIITAGILVRFPSMINDVIKGVTFGTKVNWIRFSELMIGAAILILLIVWFTRSELRIPIQYARRAQLTGKDSYLPLKIIVPGVIPVIFASTIMTIPQTILMFFNAGQNSSWYRVVQTFFTLSTTSGVIIYGLMIIFFEYLYSIVQIEPDKFADNLEKQEAYIPNVYPGDPTKEFIQNMLNYLSLPGSLFLMLVSIIPLLVANSVSSSLQIGLSGSSILIITGVLIEIGRQIKGLKLKREYGTFLSTDFSLDD

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Cyanidium caldarium
Length
410 amino acids
Function
The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
46.243 kDa
Sequence
MRPENNLRLRLFQTMKFIALERLGLFVPIPGIDQKLFSSDYSNNAISNLLNVFDNNQAPKLSVFALGIIPYINATITIQILSSAFPALKKLQSEEGEIGKKKLNKITKYLSFCFAFIESLAIVLRLQKYAFDWNLYFIVQTTLILISGAMLVMWLADNISYKGIGTGASVIIFVNIASAFAKFLLNQLFVHSIKFLDFASYFALIVFSIACIVFVQEAIRKVPIISAKQLDSTSFYSNDYFLPLRINQGGVMPIILASSLLALVDYVIRYGLSTLQAVYFINDILPFKILFLLLYSAFIIFFNYLYCSLVLNCFELSNNLKKASVVIPSIRPGKMTEKFFKDTLDNLTLFGSGFLAFIVLAPNFLEFVFHIRVFKGLAVSSLLIVVGVAIDLIKQSKTYVIAKNYENMVH

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Antithamnion sp.
Length
405 amino acids
Function
The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
45.629 kDa
Sequence
MKQPTTNKLRFTITLVILFLARVGIFIPISGIDHQTFNNTIQQNGIINFLNIFAGGGFSTIGIFALGIVPYIYASIIIQLLIKLIPYLENLQKEEGEIGRQKINQLTRYLTLLWALIQSLSIAIWINHMYLIHLFELCASLTTSSMIAMWFSEIISEYGVGNGPSLLIFQNIISSIPKNLQNYTFNIGTTNTVLNGSLILSFGIIILIINILIQEGERKIAILSAKQLGKINELNHKVIFLLKLNQGGVMPFVFASAVVHTFLFISNNTNSKITQFINLFLPNQFLYLPLYLIFIITFSYVYTSLILNPEDIAKNLKKMGASIPNIRPGSETIKYLNTRINRLTLIGACFLFTITLFPTITYYIFKINTLKGLGATSLLILVGVAIDTAKQIQTYLYHTYDNMME

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Buchnera aphidicola subsp. Acyrthosiphon kondoi
Length
356 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
38.668 kDa
Fragment
single
Sequence
MAKQPGLDFQSAKGGLGELKRRLLFVIGALIVFRIGSFIPIPGIDATVLAKLLEQQRGTIIEMFNMFSGGALSRASIFALGIMPYISASIIIQLLTVVHPALAEVKKEGEAGRRKISQYTRYGTLVLAIFQSIGIATGLPNMPGMQGLVMNPGFAFYFTAVVSLVTGTMFLMWLGEQITERGIGNGISIIIFAGIVAGLPPAVAHTIEQARQGDLHFLLLLLVAVLVFAVTFFVVFIERGQRRIVVNYAKRQQGRRVYAAQSTHLPLKVNMAGVIPAIFASSIILFPATIASWFGGGTGWNWLTTVSLYLQPGQPLYVLLYASAIIFFCFFYTALVFNPRETADNLKKSGAFVPGI

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Cyanidioschyzon merolae (strain 10D)
Length
340 amino acids
Function
The central subunit of the protein translocation channel SecYE. Consists of two halves. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug (By similarity).
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
38.022 kDa
Sequence
MQDNWPTRLAITCLLVAIERLGMYIPVGLISNPQANWLNGGGWFVLGIIPTINASIVMQILISIVPALTRLQKEEGEMGQKQIQKYTRYLTFFLAGIQAFTLSQQWCTWLLIVSGAMLVMWLAEQMTHKGIGNGTSIFVCSNIAANFLHHPIEAPWSLAMVVLIFTMLGMIALQEAVRAIPILSAKQLIQSIAQVYLLPMRLNQGGVMPIIFASSTLALLHTWSIWWLYVACIIFFSHFYNLVIANPKELSENLNKMAVVIPSIRPGAETQQYLNRTLNRMSWIGGIALSLIALLPWLFSSLKIFSGFGATSLLIVIGVSIDTMRQIRTYFIANAYEKMI

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Paracoccus denitrificans
Length
182 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently (By similarity).
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
19.854 kDa
Fragment
single
Sequence
IFASSLLLLPVTISTFSGNQTGPIMSTVLAYFGPGQPLYLLFFAAMIVFFTYFYTYNVSFKTEDVAENLKNQGGFIPGIRPGKRTEDYLTYVVTRVLVIGSAYLAFVCLLPAARDHPRPAGDPLLLGGTSVLIVVSVVMDTINQVQSHLLAHQYEGLIEKSQLPGKRGKTGAAKPRKAPARR

Gene
secY
Protein
Protein translocase subunit SecY
Organism
Geobacillus stearothermophilus
Length
99 amino acids
Function
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently (By similarity).
Similarity
Belongs to the SecY/SEC61-alpha family.
Mass
10.91 kDa
Fragment
single
Sequence
NPEQMAENLKKQGGYIPGIRPGKNTQEYVTRILYRLTLVGSVFLAVIAVLPVFFVNVANLPPSAKIGGTSLLIVVGVALETMKQLESQLVKRHYRGFIK