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Database: UniProt
Entry: A0A0J1CPW5_9BURK
LinkDB: A0A0J1CPW5_9BURK
Original site: A0A0J1CPW5_9BURK 
ID   A0A0J1CPW5_9BURK        Unreviewed;       689 AA.
AC   A0A0J1CPW5;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-SEP-2017, entry version 14.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   ORFNames=EOS_29360 {ECO:0000313|EMBL:KLU22664.1};
OS   Caballeronia mineralivorans PML1(12).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=908627 {ECO:0000313|EMBL:KLU22664.1, ECO:0000313|Proteomes:UP000035963};
RN   [1] {ECO:0000313|EMBL:KLU22664.1, ECO:0000313|Proteomes:UP000035963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PML1(12) {ECO:0000313|Proteomes:UP000035963};
RX   PubMed=26205858;
RA   Uroz S., Oger P.;
RT   "Draft Genome Sequence of Burkholderia sp. Strain PML1(12), an
RT   Ectomycorrhizosphere-Inhabiting Bacterium with Effective Mineral-
RT   Weathering Ability.";
RL   Genome Announc. 3:e00798-15(2015).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KLU22664.1}.
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DR   EMBL; AEJF01000174; KLU22664.1; -; Genomic_DNA.
DR   RefSeq; WP_047895707.1; NZ_AEJF01000174.1.
DR   EnsemblBacteria; KLU22664; KLU22664; EOS_29360.
DR   PATRIC; fig|908627.4.peg.6555; -.
DR   Proteomes; UP000035963; Unassembled WGS sequence.
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; 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   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:UP000035963};
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:UP000035963};
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      6     28       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    456    489       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    539    565       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    571    595       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   DOMAIN        1    112       SecD-TM1. {ECO:0000259|Pfam:PF13721}.
SQ   SEQUENCE   689 AA;  73270 MW;  8C729EE221F6CBAD CRC64;
     MNRYPLWKYA VMLVALVIGL VYTLPNFFGE APAVQISSGK ATVKLDSSTL ANVENALAAD
     KVTPDEVTFD NSSLNANIRV RLKDTDTQLR VKDLLQKTLN SDPSDPQYIV ALNLQAASPR
     WLTALHALPM YLGLDLRGGV HFLLQVDMAG ALNKKLDSNA ADARALLRDK NIRDGGVNRV
     NQSVVVNFAD QAAADAARTT LSTGLSELQW ATRQGGDAYQ VVGTFTPAAQ KLAEDSALKQ
     NIVTLHNRVN ELGVSEPVIQ QQGSDRIVVE LPGVQDTAKA KDIIGRTATL EARLADPTNT
     HPGPNDPVPP GDELFTQGNT GPTLVRKQVI FTGDRIIDAS SGFDEHQRPS VNIRLDAAGG
     RAVSSVSRDN IGKPMAMILF EKGKGEVLTV ATIQSELGDR FQITGQPSPQ AAADLALLLR
     AGSLAAPMDI IEERTIGPSL GADNIRKGFD SVQYGFAAIA VFMIAYYMLF GLISMLSLSV
     NLLLLIAILS MLQATLTLPG IAAIALALGM AIDANVLINE RIREELRNGA PPQLAIQNGF
     AHAWATIVDS NVTTLIAGLA LLAFGSGPVR GFAVVHCIGI LTSMFSAVFF SRGLVNLWYG
     GKKKLQSLAI GQVWRPAGSD TAAATAAYLA NQRGDDSPVD EIVQPAARAK APVPARSQKQ
     AAPAVRTGKP VARRRSGPGI EPKKPGSSN
//
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