ID B5EFS0_CITBB Unreviewed; 435 AA. AC B5EFS0; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 18-JUN-2025, entry version 87. DE RecName: Full=Protein translocase subunit SecY {ECO:0000256|ARBA:ARBA00039733, ECO:0000256|HAMAP-Rule:MF_01465}; GN Name=secY {ECO:0000256|HAMAP-Rule:MF_01465, GN ECO:0000313|EMBL:ACH37974.1}; GN OrderedLocusNames=Gbem_0953 {ECO:0000313|EMBL:ACH37974.1}; OS Citrifermentans bemidjiense (strain ATCC BAA-1014 / DSM 16622 / JCM 12645 / OS Bem) (Geobacter bemidjiensis). OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfuromonadia; OC Geobacterales; Geobacteraceae; Citrifermentans. OX NCBI_TaxID=404380 {ECO:0000313|EMBL:ACH37974.1, ECO:0000313|Proteomes:UP000008825}; RN [1] {ECO:0000313|EMBL:ACH37974.1, ECO:0000313|Proteomes:UP000008825} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1014 / DSM 16622 / JCM 12645 / Bem RC {ECO:0000313|Proteomes:UP000008825}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C., RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Lykidis A., Lovley D., Richardson P.; RT "Complete sequence of Geobacter bemidjiensis BEM."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACH37974.1, ECO:0000313|Proteomes:UP000008825} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1014 / DSM 16622 / JCM 12645 / Bem RC {ECO:0000313|Proteomes:UP000008825}; RX PubMed=20828392; DOI=10.1186/1471-2164-11-490; RA Aklujkar M., Young N.D., Holmes D., Chavan M., Risso C., Kiss H.E., RA Han C.S., Land M.L., Lovley D.R.; RT "The genome of Geobacter bemidjiensis, exemplar for the subsurface clade of RT Geobacter species that predominate in Fe(III)-reducing subsurface RT environments."; RL BMC Genomics 11:490-490(2010). 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 SecY, SecE and SecG subunits. The heterotrimers can form CC oligomers, although 1 heterotrimer is thought to be able to translocate CC proteins. Interacts with the ribosome. Interacts with SecDF, and other CC proteins may be involved. Interacts with SecA. {ECO:0000256|HAMAP- CC Rule:MF_01465}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_01465}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01465}. Membrane {ECO:0000256|ARBA:ARBA00004141, CC ECO:0000256|RuleBase:RU003484}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141, 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: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01465}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001124; ACH37974.1; -; Genomic_DNA. DR RefSeq; WP_012529386.1; NC_011146.1. DR AlphaFoldDB; B5EFS0; -. DR STRING; 404380.Gbem_0953; -. DR KEGG; gbm:Gbem_0953; -. DR eggNOG; COG0201; Bacteria. DR HOGENOM; CLU_030313_0_2_7; -. DR OrthoDB; 9809248at2; -. DR Proteomes; UP000008825; Chromosome. 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 GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-UniRule. DR FunFam; 1.10.3370.10:FF:000001; Preprotein translocase subunit SecY; 1. 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 NCBIfam; TIGR00967; 3a0501s007; 1. DR PANTHER; PTHR10906; SECY/SEC61-ALPHA FAMILY MEMBER; 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 inner membrane {ECO:0000256|HAMAP-Rule:MF_01465}; KW Cell membrane {ECO:0000256|HAMAP-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}; Reference proteome {ECO:0000313|Proteomes:UP000008825}; 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 69..94 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" FT TRANSMEM 114..133 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" FT TRANSMEM 153..172 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" FT TRANSMEM 179..200 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" FT TRANSMEM 212..234 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" FT TRANSMEM 308..328 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" FT TRANSMEM 366..385 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465" SQ SEQUENCE 435 AA; 47051 MW; F777A2B99CC01FAA CRC64; MIEAFQNIFK IPELKKKVLF SLAMLAVYRI GCHIPTPGID AQALAQFFKA AQGTLLGMFD MFSGGALEKL TVFALGIMPY ISSSIIFQLL TVVLPAVEKL SKEGDAGRKK IIQYTRYGTI VLAVVQAFGI SIGLEAMRGP AGELVVPNPG WGFRLMTVIT LTAGTAFIMW LGEQMSEKGI GNGISLIIFA GIVARIPTAI GNSFRLIKTG ELSLFVLLLI AAVMFAVIAA VVFMERGQRR IPIHYAKRVV GLKTVGAQSS HLPLKVNMAG VIPPIFASSI IMFPATVGNF IDVPWVQAAS KQLAPGKLLY EVLFVAFIVF FCYFYTAVTF NPVDVADNVK KQGGYVPGIR PGKETSDFLD AVLTKLTFAG AIYISAVCVL PSILIGKFNL PFYFGGTSLL IAVGVGMDTL SQIEAHLITR SYEGFMKGVR IQGRR //