ID   SECE_METS5              Reviewed;          59 AA.
AC   A4YH85;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Protein translocase subunit SecE {ECO:0000255|HAMAP-Rule:MF_00422};
DE   AltName: Full=Protein transport protein Sec61 gamma subunit homolog {ECO:0000255|HAMAP-Rule:MF_00422};
GN   Name=secE {ECO:0000255|HAMAP-Rule:MF_00422}; OrderedLocusNames=Msed_1632;
OS   Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS   / TH2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=399549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX   PubMed=18083856; DOI=10.1128/aem.02019-07;
RA   Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT   "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT   archaeon Metallosphaera sedula provides insights into bioleaching-
RT   associated metabolism.";
RL   Appl. Environ. Microbiol. 74:682-692(2008).
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 (alpha), SecG (beta) and SecE (gamma) 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:0000255|HAMAP-Rule:MF_00422}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00422};
CC       Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00422}.
CC   -!- SIMILARITY: Belongs to the SecE/SEC61-gamma family. {ECO:0000255|HAMAP-
CC       Rule:MF_00422}.
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DR   EMBL; CP000682; ABP95787.1; -; Genomic_DNA.
DR   RefSeq; WP_012021574.1; NC_009440.1.
DR   AlphaFoldDB; A4YH85; -.
DR   SMR; A4YH85; -.
DR   STRING; 399549.Msed_1632; -.
DR   EnsemblBacteria; ABP95787; ABP95787; Msed_1632.
DR   GeneID; 5104837; -.
DR   GeneID; 59457255; -.
DR   KEGG; mse:Msed_1632; -.
DR   eggNOG; arCOG02204; Archaea.
DR   HOGENOM; CLU_191921_1_0_2; -.
DR   OMA; DWKRIIT; -.
DR   Proteomes; UP000000242; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008320; F:protein transmembrane 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   Gene3D; 1.20.5.820; -; 1.
DR   HAMAP; MF_00422; SecE; 1.
DR   InterPro; IPR023391; Prot_translocase_SecE_dom_sf.
DR   InterPro; IPR001901; Translocase_SecE/Sec61-g.
DR   SUPFAM; SSF103456; SSF103456; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Protein transport; Reference proteome;
KW   Translocation; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..59
FT                   /note="Protein translocase subunit SecE"
FT                   /id="PRO_1000072301"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00422"
SQ   SEQUENCE   59 AA;  6776 MW;  7D0770B9B8543EA9 CRC64;
     MGLADRIKKL REDWKRIISV AKKPDKSMFY LNLRVTLIVL LFVGLLAFLV QLAFSILLG