ID A0A2A2HB52_9EURY Unreviewed; 449 AA.
AC A0A2A2HB52;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000256|HAMAP-Rule:MF_01465, ECO:0000256|RuleBase:RU000537};
DE AltName: Full=Protein transport protein SEC61 subunit alpha homolog {ECO:0000256|HAMAP-Rule:MF_01465};
GN Name=secY {ECO:0000256|HAMAP-Rule:MF_01465};
GN ORFNames=ASJ82_04255 {ECO:0000313|EMBL:PAV06649.1};
OS Methanosphaera cuniculi.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=1077256 {ECO:0000313|EMBL:PAV06649.1, ECO:0000313|Proteomes:UP000217528};
RN [1] {ECO:0000313|EMBL:PAV06649.1, ECO:0000313|Proteomes:UP000217528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1R-7 {ECO:0000313|EMBL:PAV06649.1,
RC ECO:0000313|Proteomes:UP000217528};
RX PubMed=28826405; DOI=10.1186/s12864-017-4036-4;
RA Gilmore S.P., Henske J.K., Sexton J.A., Solomon K.V., Seppala S., Yoo J.I.,
RA Huyett L.M., Pressman A., Cogan J.Z., Kivenson V., Peng X., Tan Y.,
RA Valentine D.L., O'Malley M.A.;
RT "Genomic analysis of methanogenic archaea reveals a shift towards energy
RT conservation.";
RL BMC Genomics 18:639-639(2017).
CC -!- FUNCTION: The central subunit of the protein translocation channel
CC SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two
CC domains form a lateral gate at the front which open onto the bilayer
CC between TMs 2 and 7, and are clamped together by SecE at the back. The
CC channel is closed by both a pore ring composed of hydrophobic SecY
CC resides and a short helix (helix 2A) on the extracellular side of the
CC membrane which forms a plug. The plug probably moves laterally to allow
CC the channel to open. The ring and the pore may move independently.
CC {ECO:0000256|HAMAP-Rule:MF_01465, ECO:0000256|RuleBase:RU000537}.
CC -!- SUBUNIT: Component of the Sec protein translocase complex. Heterotrimer
CC consisting of alpha (SecY), beta (SecG) and gamma (SecE) subunits. The
CC heterotrimers can form oligomers, although 1 heterotrimer is thought to
CC be able to translocate proteins. Interacts with the ribosome. May
CC interact with SecDF, and other proteins may be involved.
CC {ECO:0000256|HAMAP-Rule:MF_01465}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01465};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01465}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003484}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU003484}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family.
CC {ECO:0000256|ARBA:ARBA00005751, ECO:0000256|HAMAP-Rule:MF_01465,
CC ECO:0000256|RuleBase:RU004349}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PAV06649.1}.
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DR EMBL; LMVN01000027; PAV06649.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2HB52; -.
DR OrthoDB; 371914at2157; -.
DR Proteomes; UP000217528; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.3370.10; SecY subunit domain; 1.
DR HAMAP; MF_01465; SecY; 1.
DR InterPro; IPR026593; SecY.
DR InterPro; IPR002208; SecY/SEC61-alpha.
DR InterPro; IPR030659; SecY_CS.
DR InterPro; IPR023201; SecY_dom_sf.
DR InterPro; IPR019561; Translocon_Sec61/SecY_plug_dom.
DR NCBIfam; TIGR00967; 3a0501s007; 1.
DR PANTHER; PTHR10906:SF1; DSEC61ALPHA; 1.
DR PANTHER; PTHR10906; SECY/SEC61-ALPHA FAMILY MEMBER; 1.
DR Pfam; PF10559; Plug_translocon; 1.
DR Pfam; PF00344; SecY; 1.
DR PIRSF; PIRSF004557; SecY; 1.
DR PRINTS; PR00303; SECYTRNLCASE.
DR SUPFAM; SSF103491; Preprotein translocase SecY subunit; 1.
DR PROSITE; PS00755; SECY_1; 1.
DR PROSITE; PS00756; SECY_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01465};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01465};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW Rule:MF_01465};
KW Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW Rule:MF_01465};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01465};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01465};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01465}.
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 70..94
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 115..136
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 142..160
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 172..193
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 219..238
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 328..347
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 385..403
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 409..427
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT DOMAIN 38..71
FT /note="Translocon Sec61/SecY plug"
FT /evidence="ECO:0000259|Pfam:PF10559"
SQ SEQUENCE 449 AA; 48495 MW; C95A5EE532C61773 CRC64;
MSSLDSIKPF YSLLPHVATP KGHVDFKDKL KWTGIILILY FLLTEVSLFG LSPTAIDQFA
QLRSVMAGSF GSIITLGIGP IVTASIVMQL LVGGKLINLD LSKPEDKSAF QGTQKLLAII
FTLFEGIILV FTGSLPPISD EYTLILIIQM VLGGILIIYM DEVVSKWGFG SGIGLFIAAG
VAEQILVGTF NFLPATGTNV PAGKLPAFIY SLMVGQPNFS LLIPIIATIA VFLIVVYAEC
MRVEIPLSYG GVKGARSKYP LKFVYASNMP VILVSALFLN VQLFAGLFQS IGFPILGEVS
QGQPISGVAY YLTTPSSISV LFTDPLRVLI YAIVFVGLCI LFALLWVEIS GIGPKQVAKQ
LSEMGVQIPG FRNSKVHFRK IMDKYIPPIT VLGGAFVGLL AFGADLTGAL GGGTGVLLTV
GIVYRLYEDI AKEQLMDMHP MMRRFFGNE
//
