ID SECE_BUCAI Reviewed; 127 AA. AC P57152; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 04-NOV-2026, entry version 119. DE RecName: Full=Protein translocase subunit SecE {ECO:0000255|HAMAP-Rule:MF_00422}; GN Name=secE {ECO:0000255|HAMAP-Rule:MF_00422}; OrderedLocusNames=BU040; OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon OS pisum symbiotic bacterium). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Erwiniaceae; Buchnera. OX NCBI_TaxID=107806; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=APS; RX PubMed=10993077; DOI=10.1038/35024074; RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.; RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera RT sp. APS."; RL Nature 407:81-86(2000). CC -!- FUNCTION: Essential subunit of the Sec protein translocation channel CC SecYEG. Clamps together the 2 halves of SecY. May contact the channel CC plug during translocation. {ECO:0000255|HAMAP-Rule:MF_00422}. 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_00422}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00422}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00422}. CC -!- SIMILARITY: Belongs to the SecE/SEC61-gamma family. {ECO:0000255|HAMAP- CC Rule:MF_00422}. 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; BA000003; BAB12767.1; -; Genomic_DNA. DR RefSeq; WP_010895914.1; NC_002528.1. DR AlphaFoldDB; P57152; -. DR STRING; 563178.BUAP5A_039; -. DR EnsemblBacteria; BAB12767; BAB12767; BAB12767. DR KEGG; buc:BU040; -. DR PATRIC; fig|107806.10.peg.53; -. DR eggNOG; COG0690; Bacteria. DR HOGENOM; CLU_113663_0_1_6; -. DR OMA; AFVCTYY; -. DR Proteomes; UP000001806; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008320; F:transmembrane protein transporter activity; IEA:UniProtKB-UniRule. DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule. DR GO; GO:0009306; P:protein secretion; 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; 1.20.5.1030; Preprotein translocase secy subunit; 1. DR HAMAP; MF_00422; SecE; 1. DR InterPro; IPR005807; SecE_bac. DR InterPro; IPR038379; SecE_sf. DR InterPro; IPR001901; Translocase_SecE/Sec61-g. DR NCBIfam; TIGR00964; secE_bact; 1. DR PANTHER; PTHR33910; PROTEIN TRANSLOCASE SUBUNIT SECE; 1. DR PANTHER; PTHR33910:SF1; PROTEIN TRANSLOCASE SUBUNIT SECE; 1. DR Pfam; PF00584; SecE; 1. DR PRINTS; PR01650; SECETRNLCASE. 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..127 FT /note="Protein translocase subunit SecE" FT /id="PRO_0000104160" FT TRANSMEM 17..37 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00422" FT TRANSMEM 41..61 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00422" FT TRANSMEM 95..115 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00422" SQ SEQUENCE 127 AA; 15326 MW; 58E6DF4E77B4FA5D CRC64; MNKHHYNRNK HKIPEKVKWI SISIFFILSF FINMCFYETQ LFIRIFIISC LMLCAIGTMI YTKKGKDILL YIVMSKKEMQ KIIWPKYKET LYTTFIVISV TIFISFILWS IDSVIFRLIA FIISLRF //