SECE_METAC
ID SECE_METAC Reviewed; 71 AA.
AC Q8TI84;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Protein translocase subunit SecE {ECO:0000255|HAMAP-Rule:MF_00422};
DE AltName: Full=Protein transport protein Sec61 gamma subunit homolog {ECO:0000255|HAMAP-Rule:MF_00422};
GN Name=secE {ECO:0000255|HAMAP-Rule:MF_00422}; OrderedLocusNames=MA_4272;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
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 (alpha), SecG (beta) and SecE (gamma) subunits. The
CC heterotrimers can form oligomers, although 1 heterotrimer is thought to
CC be able to translocate proteins. Interacts with the ribosome. May
CC interact with SecDF, and other proteins may be involved.
CC {ECO:0000255|HAMAP-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; AE010299; AAM07616.1; -; Genomic_DNA.
DR RefSeq; WP_011024153.1; NC_003552.1.
DR AlphaFoldDB; Q8TI84; -.
DR SMR; Q8TI84; -.
DR STRING; 188937.MA_4272; -.
DR EnsemblBacteria; AAM07616; AAM07616; MA_4272.
DR GeneID; 1476166; -.
DR KEGG; mac:MA_4272; -.
DR HOGENOM; CLU_191921_2_1_2; -.
DR InParanoid; Q8TI84; -.
DR OMA; LTMLPQW; -.
DR OrthoDB; 121918at2157; -.
DR Proteomes; UP000002487; 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 Gene3D; 1.20.5.820; -; 1.
DR HAMAP; MF_00422; SecE; 1.
DR InterPro; IPR023391; Prot_translocase_SecE_dom_sf.
DR InterPro; IPR008158; Translocase_Sec61-g.
DR InterPro; IPR001901; Translocase_SecE/Sec61-g.
DR Pfam; PF00584; SecE; 1.
DR SUPFAM; SSF103456; SSF103456; 1.
DR TIGRFAMs; TIGR00327; secE_euk_arch; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..71
FT /note="Protein translocase subunit SecE"
FT /id="PRO_0000104218"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00422"
SQ SEQUENCE 71 AA; 7753 MW; 0E0956FA70E5BAD7 CRC64;
MVESTFEPNI TTKSVGQAIR AHLRVLKLTK KPSREEFLTI AKVAGAGILA VGAIGFIIYV
LLTMLPQWVS Q