ID   SECE_THET8              Reviewed;          60 AA.
AC   P38383; Q5SLP4;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 2.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=Protein translocase subunit SecE {ECO:0000255|HAMAP-Rule:MF_00422};
GN   Name=secE {ECO:0000255|HAMAP-Rule:MF_00422}; OrderedLocusNames=TTHA0249;
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RX   PubMed=1447157; DOI=10.1128/jb.174.23.7859-7863.1992;
RA   Heinrich T., Schroeder W., Erdmann V.A., Hartmann R.K.;
RT   "Identification of the gene encoding transcription factor NusG of Thermus
RT   thermophilus.";
RL   J. Bacteriol. 174:7859-7863(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 3-434 OF THE SECYE COMPLEX WITH A
RP   PARTIALLY OPEN LATERAL GATE, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=18923527; DOI=10.1038/nature07421;
RA   Tsukazaki T., Mori H., Fukai S., Ishitani R., Mori T., Dohmae N.,
RA   Perederina A., Sugita Y., Vassylyev D.G., Ito K., Nureki O.;
RT   "Conformational transition of Sec machinery inferred from bacterial SecYE
RT   structures.";
RL   Nature 455:988-991(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:18923527}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00422, ECO:0000269|PubMed:18923527}; Single-pass membrane
CC       protein {ECO:0000255|HAMAP-Rule:MF_00422, ECO:0000269|PubMed:18923527}.
CC   -!- SIMILARITY: Belongs to the SecE/SEC61-gamma family. {ECO:0000255|HAMAP-
CC       Rule:MF_00422}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=L10348; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; L10348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP008226; BAD70072.1; -; Genomic_DNA.
DR   RefSeq; WP_008630510.1; NC_006461.1.
DR   RefSeq; YP_143515.1; NC_006461.1.
DR   PDB; 2ZJS; X-ray; 3.20 A; E=1-60.
DR   PDB; 2ZQP; X-ray; 6.00 A; E=1-60.
DR   PDB; 5AWW; X-ray; 2.72 A; E=1-60.
DR   PDB; 5CH4; X-ray; 3.64 A; E=1-60.
DR   PDBsum; 2ZJS; -.
DR   PDBsum; 2ZQP; -.
DR   PDBsum; 5AWW; -.
DR   PDBsum; 5CH4; -.
DR   AlphaFoldDB; P38383; -.
DR   SMR; P38383; -.
DR   STRING; 300852.55771631; -.
DR   EnsemblBacteria; BAD70072; BAD70072; BAD70072.
DR   GeneID; 3168489; -.
DR   KEGG; ttj:TTHA0249; -.
DR   eggNOG; COG0690; Bacteria.
DR   HOGENOM; CLU_113663_8_0_0; -.
DR   OMA; MNLIQYF; -.
DR   EvolutionaryTrace; P38383; -.
DR   Proteomes; UP000000532; 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   Pfam; PF00584; SecE; 1.
DR   TIGRFAMs; TIGR00964; secE_bact; 1.
DR   PROSITE; PS01067; SECE_SEC61G; 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..60
FT                   /note="Protein translocase subunit SecE"
FT                   /id="PRO_0000104189"
FT   TOPO_DOM        1..31
FT                   /note="Cytoplasmic"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT   TOPO_DOM        53..60
FT                   /note="Extracellular"
FT   CONFLICT        44
FT                   /note="I -> Y (in Ref. 1; L10348)"
FT                   /evidence="ECO:0000305"
FT   HELIX           2..17
FT                   /evidence="ECO:0007829|PDB:5AWW"
FT   HELIX           24..59
FT                   /evidence="ECO:0007829|PDB:5AWW"
SQ   SEQUENCE   60 AA;  7065 MW;  0B7BEA730CB3ADBD CRC64;
     MFARLIRYFQ EARAELARVT WPTREQVVEG TQAILLFTLA FMVILGLYDT VFRFLIGLLR