ID   SECE_STAEQ              Reviewed;          60 AA.
AC   Q5HRL7;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Protein translocase subunit SecE {ECO:0000255|HAMAP-Rule:MF_00422};
GN   Name=secE {ECO:0000255|HAMAP-Rule:MF_00422}; OrderedLocusNames=SERP0176;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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 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; CP000029; AAW53566.1; -; Genomic_DNA.
DR   RefSeq; WP_002438679.1; NC_002976.3.
DR   AlphaFoldDB; Q5HRL7; -.
DR   SMR; Q5HRL7; -.
DR   STRING; 176279.SERP0176; -.
DR   EnsemblBacteria; AAW53566; AAW53566; SERP0176.
DR   GeneID; 50019536; -.
DR   KEGG; ser:SERP0176; -.
DR   eggNOG; COG0690; Bacteria.
DR   HOGENOM; CLU_113663_8_2_9; -.
DR   OMA; EMKRVSW; -.
DR   OrthoDB; 1974284at2; -.
DR   Proteomes; UP000000531; 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   GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.5.1030; -; 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   PANTHER; PTHR33910; PTHR33910; 1.
DR   Pfam; PF00584; SecE; 1.
DR   TIGRFAMs; TIGR00964; secE_bact; 1.
DR   PROSITE; PS01067; SECE_SEC61G; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Protein transport; Reference proteome;
KW   Translocation; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..60
FT                   /note="Protein translocase subunit SecE"
FT                   /id="PRO_0000104182"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00422"
SQ   SEQUENCE   60 AA;  6973 MW;  40D8E8C9ABC9644D CRC64;
     MAKKESFFKG VKSEMEKTSW PTKEELFKYT IIVVSTVIFF LVFFYALDIG INALKQLFLG