ID   SECE_MYCLE              Reviewed;         146 AA.
AC   Q9CBJ9;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Protein translocase subunit SecE {ECO:0000255|HAMAP-Rule:MF_00422};
GN   Name=secE {ECO:0000255|HAMAP-Rule:MF_00422}; OrderedLocusNames=ML1907;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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; AL583923; CAC30861.1; -; Genomic_DNA.
DR   PIR; E87147; E87147.
DR   RefSeq; NP_302284.1; NC_002677.1.
DR   RefSeq; WP_010908605.1; NC_002677.1.
DR   AlphaFoldDB; Q9CBJ9; -.
DR   SMR; Q9CBJ9; -.
DR   STRING; 272631.ML1907; -.
DR   EnsemblBacteria; CAC30861; CAC30861; CAC30861.
DR   KEGG; mle:ML1907; -.
DR   PATRIC; fig|272631.5.peg.3615; -.
DR   Leproma; ML1907; -.
DR   eggNOG; COG0690; Bacteria.
DR   HOGENOM; CLU_113663_1_2_11; -.
DR   OMA; PNRKQMI; -.
DR   Proteomes; UP000000806; 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..146
FT                   /note="Protein translocase subunit SecE"
FT                   /id="PRO_0000104167"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00422"
FT   REGION          1..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   146 AA;  15749 MW;  3F802561AE51CC4B CRC64;
     MSDERYAASD GGGTEVGSGT RGRTTVVTKP ATRPQRPTGK RSRQRAANAS NTGANVEVEE
     SSTQAAIAKE GKVKKPKKSA DRSANPIVFI YNYLKQVVGE MRKVIWPNRK QMLTYTSVVL
     AFLAFMVALV GLADFGLAKL VLLVFG