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Database: UniProt
Entry: M4R9G2_BIBTR
LinkDB: M4R9G2_BIBTR
Original site: M4R9G2_BIBTR 
ID   M4R9G2_BIBTR            Unreviewed;       614 AA.
AC   M4R9G2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-SEP-2017, entry version 27.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   ORFNames=WQG_15460 {ECO:0000313|EMBL:AGH38823.1};
OS   Bibersteinia trehalosi USDA-ARS-USMARC-192.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Bibersteinia.
OX   NCBI_TaxID=1171377 {ECO:0000313|EMBL:AGH38823.1, ECO:0000313|Proteomes:UP000011846};
RN   [1] {ECO:0000313|EMBL:AGH38823.1, ECO:0000313|Proteomes:UP000011846}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=192 {ECO:0000313|Proteomes:UP000011846};
RA   Harhay G.P., Koren S., Phillippy A., McVey D.S., Kuszak J.,
RA   Clawson M., Harhay D.M., Heaton M., Chitko-Mckown C., Smith T.P.L.;
RT   "Annotation of the Bibersteinia trehalsoi USDA-ARS-USMARC-192 complete
RT   genome.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of the Sec protein translocase complex. Interacts
CC       with the SecYEG preprotein conducting channel. SecDF uses the
CC       proton motive force (PMF) to complete protein translocation after
CC       the ATP-dependent function of SecA. {ECO:0000256|HAMAP-
CC       Rule:MF_01463, ECO:0000256|SAAS:SAAS00541769}.
CC   -!- SUBUNIT: Forms a complex with SecF. Part of the essential Sec
CC       protein translocation apparatus which comprises SecA, SecYEG and
CC       auxiliary proteins SecDF-YajC and YidC. {ECO:0000256|HAMAP-
CC       Rule:MF_01463}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01463}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01463}.
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01463}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01463}.
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DR   EMBL; CP003745; AGH38823.1; -; Genomic_DNA.
DR   EnsemblBacteria; AGH38823; AGH38823; WQG_15460.
DR   KEGG; bto:WQG_15460; -.
DR   PATRIC; fig|1171377.3.peg.1536; -.
DR   KO; K03072; -.
DR   OrthoDB; POG091H02C5; -.
DR   Proteomes; UP000011846; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005622; C:intracellular; IEA:GOC.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015450; F:P-P-bond-hydrolysis-driven protein transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0065002; P:intracellular protein transmembrane transport; 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   HAMAP; MF_01463_B; SecD_B; 1.
DR   InterPro; IPR001036; Acrflvin-R.
DR   InterPro; IPR005791; SecD.
DR   InterPro; IPR027398; SecD-TM.
DR   InterPro; IPR022813; SecD/SecF_arch_bac.
DR   InterPro; IPR022645; SecD/SecF_bac.
DR   InterPro; IPR022646; SecD/SecF_CS.
DR   Pfam; PF07549; Sec_GG; 1.
DR   Pfam; PF13721; SecD-TM1; 1.
DR   Pfam; PF02355; SecD_SecF; 1.
DR   PRINTS; PR00702; ACRIFLAVINRP.
DR   TIGRFAMs; TIGR00916; 2A0604s01; 1.
DR   TIGRFAMs; TIGR01129; secD; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425060};
KW   Complete proteome {ECO:0000313|Proteomes:UP000011846};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00284057};
KW   Protein transport {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425133};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011846};
KW   Translocation {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425069};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425065};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425143};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425109}.
FT   TRANSMEM    456    474       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    481    499       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    505    524       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    545    569       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    581    604       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   DOMAIN        2    103       SecD-TM1. {ECO:0000259|Pfam:PF13721}.
SQ   SEQUENCE   614 AA;  66611 MW;  5C8AEF1CB5E9F367 CRC64;
     MLNRFPLWKN LMVILVIAIG ALYALPNLYG EDPSVQISGT RGQQTSQETL TQVQSALSAL
     NITPKAMSLE NGSILVRLNK DEEQLPAKEK IAEVLGNNYS VALNLAPATP EWLTSIGGEP
     MKRGLDLRGG VRFLMEVDMN TALTKQQDQL QDSLRAIFRK DNIETKSFKK VDNFGTEIEF
     NDENGAEKAV RYIRRTYPTL DVLLTSTNVA VLTPSAQGLS ESRDLAIEQN LTILRKRVEE
     LGVSEPTIQR QGADRIVVEL PGVQDTARAK EILGATATLE FRMVNQEADL GQASRGIVPL
     NSELKYDRHG GPVVLRMRPS LGGEHIINAK SGIDERGLPQ VSIELDSEGG SLMGEITKSE
     VGKPMATLYS EFKDSGKRDA NGKVILEKHE EVINVATINS RLGSHFQITG INSPAEAQNL
     AVLLRSGALI APIVIVEERT IGASLGADNI AQGMEAGLLG LSLTLIFCLV YYKVFGIFAS
     MALIVNLILT VGLMSLIGAT LTMPGIAGIV LAVGMSIDAN VLIYERIKEE MRNGRSIQQA
     IHEGYDGAFS SIFDSNLTTI LTSLILYAVG TGPVKGFAVT LALGVMISMF TAITGTRMLV
     NWVYGGKRVK KLWI
//
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