ID   SECE_AQUAE              Reviewed;          65 AA.
AC   D0VWU4;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Protein translocase subunit SecE {ECO:0000255|HAMAP-Rule:MF_00422};
GN   Name=secE {ECO:0000255|HAMAP-Rule:MF_00422}; OrderedLocusNames=aq_1930;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (7.5 ANGSTROMS) OF SECYEG IN COMPLEX WITH B.SUBTILIS
RP   SECA.
RX   PubMed=18923516; DOI=10.1038/nature07335;
RA   Zimmer J., Nam Y., Rapoport T.A.;
RT   "Structure of a complex of the ATPase SecA and the protein-translocation
RT   channel.";
RL   Nature 455:936-943(2008).
CC   -!- FUNCTION: Essential subunit of the protein translocation channel
CC       SecYEG. Clamps together the 2 halves of SecY. May contact the channel
CC       plug during translocation.
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 SecDF, and other proteins may be involved. The
CC       channel interacts with SecA via subunit SecY.
CC       {ECO:0000269|PubMed:18923516}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the SecE/SEC61-gamma family. {ECO:0000255|HAMAP-
CC       Rule:MF_00422}.
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DR   EMBL; AE000657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_214325.1; NC_000918.1.
DR   RefSeq; WP_010881261.1; NC_000918.1.
DR   PDB; 3DL8; X-ray; 7.50 A; C/D=1-65.
DR   PDBsum; 3DL8; -.
DR   AlphaFoldDB; D0VWU4; -.
DR   SMR; D0VWU4; -.
DR   IntAct; D0VWU4; 3.
DR   KEGG; aae:aq_1930b; -.
DR   OrthoDB; 1974284at2; -.
DR   EvolutionaryTrace; D0VWU4; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central.
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; IBA:GO_Central.
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.
PE   1: Evidence at protein level;
KW   3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW   Protein transport; Reference proteome; Translocation; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..65
FT                   /note="Protein translocase subunit SecE"
FT                   /id="PRO_0000414188"
FT   TOPO_DOM        1..27
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        28..59
FT                   /note="Helical"
FT   TOPO_DOM        60..65
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   65 AA;  7494 MW;  4571C9039CF613DF CRC64;
     MEKLKEFLKG VRDELKRVVW PSRELVVKAT ISVIIFSLAI GVYLWILDLT FTKIISFILS
     LRGSL