ID   SECE_VIBAL              Reviewed;         126 AA.
AC   Q9ZNE7;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Protein translocase subunit SecE {ECO:0000255|HAMAP-Rule:MF_00422};
GN   Name=secE {ECO:0000255|HAMAP-Rule:MF_00422};
OS   Vibrio alginolyticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9791006; DOI=10.1006/bbrc.1998.9573;
RA   Nishiyama K., Furuta M., Tokuda H.;
RT   "Molecular cloning and functional characterization of SecE of a marine
RT   bacterium, Vibrio alginolyticus.";
RL   Biochem. Biophys. Res. Commun. 251:894-897(1998).
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}.
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DR   EMBL; AB016766; BAA34065.1; -; Genomic_DNA.
DR   PIR; JE0331; JE0331.
DR   AlphaFoldDB; Q9ZNE7; -.
DR   STRING; 663.BAU10_24160; -.
DR   eggNOG; COG0690; Bacteria.
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   PRINTS; PR01650; SECETRNLCASE.
DR   TIGRFAMs; TIGR00964; secE_bact; 1.
DR   PROSITE; PS01067; SECE_SEC61G; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW   Translocation; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..126
FT                   /note="Protein translocase subunit SecE"
FT                   /id="PRO_0000104192"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00422"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00422"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00422"
SQ   SEQUENCE   126 AA;  13182 MW;  89533DB58F3ABBB9 CRC64;
     MKANNAETPD SSNAADTFKW LAAFVLAAAA VVGNYLYGEM SVVVRAAGVV VLIAAALGVA
     ATTTKGKAAI SFAKESRMEV RKVVWPTRQE TMQTTLIVLA VSIVMALVLW GIDGIMVRLV
     ALATGV