ID SECY_RICPR Reviewed; 433 AA. AC Q9ZCS5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 109. DE RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465}; GN Name=secY {ECO:0000255|HAMAP-Rule:MF_01465}; OrderedLocusNames=RP639; OS Rickettsia prowazekii (strain Madrid E). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group. OX NCBI_TaxID=272947; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Madrid E; RX PubMed=9823893; DOI=10.1038/24094; RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., RA Kurland C.G.; RT "The genome sequence of Rickettsia prowazekii and the origin of RT mitochondria."; RL Nature 396:133-140(1998). 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:0000255|HAMAP-Rule:MF_01465}. 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:0000255|HAMAP- CC Rule:MF_01465}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01465}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01465}. CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000255|HAMAP- CC 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; AJ235272; CAA15079.1; -; Genomic_DNA. DR PIR; E71669; E71669. DR RefSeq; NP_221003.1; NC_000963.1. DR RefSeq; WP_004596233.1; NC_000963.1. DR AlphaFoldDB; Q9ZCS5; -. DR SMR; Q9ZCS5; -. DR STRING; 272947.gene:17555716; -. DR EnsemblBacteria; CAA15079; CAA15079; CAA15079. DR GeneID; 57569764; -. DR KEGG; rpr:RP639; -. DR PATRIC; fig|272947.5.peg.661; -. DR eggNOG; COG0201; Bacteria. DR HOGENOM; CLU_030313_0_2_5; -. DR OrthoDB; 9809248at2; -. DR Proteomes; UP000002480; 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 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:SF9; PREPROTEIN TRANSLOCASE SUBUNIT SCY1, CHLOROPLASTIC; 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; Cell membrane; Membrane; Protein transport; KW Reference proteome; Translocation; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1..433 FT /note="Protein translocase subunit SecY" FT /id="PRO_0000131738" FT TRANSMEM 17..37 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465" FT TRANSMEM 71..91 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465" FT TRANSMEM 117..137 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465" FT TRANSMEM 149..169 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465" FT TRANSMEM 184..204 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465" FT TRANSMEM 212..232 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465" FT TRANSMEM 268..288 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465" FT TRANSMEM 310..330 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465" FT TRANSMEM 366..386 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465" FT TRANSMEM 388..408 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465" SQ SEQUENCE 433 AA; 47697 MW; DE2FF632BA24A0A5 CRC64; MGQNFSKKSS NDLVNRIIFT LFMLIICRFG SFIPIPGIDS IALNSVAEKN QFGILGMFNM LSGGSLGRMS IFALAIMPYI TASIIIQLMS VAYKPLENLK KEGETGKRKI NQLSRYLTVL LASFQAYGVA LSLESMVTNT GPVVILAGFF FRVTTVITLV VGTILLMWLG EQITQRGIGN GTSLIIFIGI ISGVPSAIIS MFELSRKGAL SPLIAITVCI GVVLLIAIII FFEKAQRKLL VQYPKRQVGN KIYGGEATHM PLKLNTSGVI PPIFASSILL FPTTLASFSN SNSDTMSMLT YYLGHGKPVY ILLYVVLIMF FSFFYTAIVF NSEETANNLR KYGAYIPGKR PGKNTSDYFD YILTRLTVIG GIYLSVICVI PELLMNKYVI SLSLGGTSFL IVVNVVLDTM TQIQTYLFSS KYEGLMKKIK LKN //