SECE_METBF
ID SECE_METBF Reviewed; 71 AA.
AC Q46EU5;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 108.
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=Mbar_A0617;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ69597.1; -; Genomic_DNA.
DR RefSeq; WP_011305648.1; NC_007355.1.
DR AlphaFoldDB; Q46EU5; -.
DR SMR; Q46EU5; -.
DR STRING; 269797.Mbar_A0617; -.
DR EnsemblBacteria; AAZ69597; AAZ69597; Mbar_A0617.
DR GeneID; 3627677; -.
DR KEGG; mba:Mbar_A0617; -.
DR eggNOG; arCOG02204; Archaea.
DR HOGENOM; CLU_191921_2_1_2; -.
DR OMA; LTMLPQW; -.
DR OrthoDB; 121918at2157; -.
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; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..71
FT /note="Protein translocase subunit SecE"
FT /id="PRO_0000273137"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00422"
SQ SEQUENCE 71 AA; 7806 MW; B909F1CA88F29971 CRC64;
MVESTFEPKI TAESVGQVIR AHLRVLKLTR KPSREEFLTI AKVAGVGILA VGAIGFIIYV
LLTMLPQWVA Q