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Database: UniProt
Entry: A0A084UAA5_9RHIZ
LinkDB: A0A084UAA5_9RHIZ
Original site: A0A084UAA5_9RHIZ 
ID   A0A084UAA5_9RHIZ        Unreviewed;       850 AA.
AC   A0A084UAA5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   25-OCT-2017, entry version 21.
DE   RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_01463, ECO:0000256|HAMAP-Rule:MF_01464};
DE   Includes:
DE     RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
DE   Includes:
DE     RecName: Full=Protein-export membrane protein SecF {ECO:0000256|HAMAP-Rule:MF_01464};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Synonyms=secF {ECO:0000256|HAMAP-Rule:MF_01464};
GN   ORFNames=EL18_00913 {ECO:0000313|EMBL:KFB09891.1};
OS   Nitratireductor basaltis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Nitratireductor.
OX   NCBI_TaxID=472175 {ECO:0000313|EMBL:KFB09891.1, ECO:0000313|Proteomes:UP000053675};
RN   [1] {ECO:0000313|EMBL:KFB09891.1, ECO:0000313|Proteomes:UP000053675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMTGB225 {ECO:0000313|EMBL:KFB09891.1,
RC   ECO:0000313|Proteomes:UP000053675};
RA   Gan H.Y.;
RT   "Draft Genome Sequence of Nitratireductor basaltis Strain UMTGB225, A
RT   Marine Bacterium Isolated from Green Barrel Tunicate.";
RL   Submitted (MAY-2014) 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 SecD. 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_01464}.
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   -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01464}.
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:KFB09891.1}.
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DR   EMBL; JMQM01000001; KFB09891.1; -; Genomic_DNA.
DR   RefSeq; WP_036480185.1; NZ_JMQM01000001.1.
DR   EnsemblBacteria; KFB09891; KFB09891; EL18_00913.
DR   PATRIC; fig|472175.3.peg.925; -.
DR   Proteomes; UP000053675; 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   HAMAP; MF_01464_B; SecF_B; 1.
DR   InterPro; IPR005791; SecD.
DR   InterPro; IPR022813; SecD/SecF_arch_bac.
DR   InterPro; IPR022645; SecD/SecF_bac.
DR   InterPro; IPR022646; SecD/SecF_CS.
DR   InterPro; IPR005665; SecF_bac.
DR   Pfam; PF07549; Sec_GG; 2.
DR   Pfam; PF02355; SecD_SecF; 2.
DR   PRINTS; PR01755; SECFTRNLCASE.
DR   TIGRFAMs; TIGR00916; 2A0604s01; 2.
DR   TIGRFAMs; TIGR00966; 3a0501s07; 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:UP000053675};
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:UP000053675};
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    376    393       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    398    420       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    466    491       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    497    521       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    555    574       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    670    691       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    698    721       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    727    746       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    767    793       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    805    827       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
SQ   SEQUENCE   850 AA;  91788 MW;  3CEEE4E3C064AFE5 CRC64;
     MLYFPRWQTV LIWLAVALGI AYAAPNILPQ TWFSSMPTWA PKQPMTLGLD LQGGSHILLA
     LDRDELTEER LVSARDDVRR SLREERIGYT GLAINGQAVQ VRVRDASQLD AAREALSELT
     QPVSSGVFGS GAVAEFSLSE PEQGILRYSL TEQGIEYRLN SALSQSIEVV SRRVNELGTT
     EPVIQRQGDD RILVQVPGLQ DPERLKEILG QTAKLTFQMV DQSMPAQEAI EGRPPVGTSV
     MYSTDDPPVP YVIEDRIIVS GENLVDAQAS FDQRTNEPVV SFRFDTRGAT GFGQATQENV
     GRLFAIILDG QVISAPQIRE PILGGSGQIS GNFSVQGAND LAVLLRAGAL PATLTVIEER
     TVGPGLGQDS INAGKIAAMI GAVLVVAFMI IAYGTFGVFA VVALGANIAL IIALLSGLGA
     TLTLPGIAGI VLTMGMAVDS NVLVFERIRE ERANGRSLIQ AVDSGFSKAL GTIVDANVTT
     LIAAIILFYL GTGPVRGFAV TLAIGIATTV FTAYTLTRWL VAQWVKRQRP KELPRAPLNL
     LPGATSIGFM WLRRMTFTLS AIASIAALAL FMTLNMNYGI DFKGGSAIEV QARQDVADIS
     DIRSRLSELN LGEVQVQEFG NPKDVLIRVQ AQGGGEQAEQ TVITKVRDAL EADYDFRRVE
     VVGPTVSGEL ARAGTIAVLV SLFAILIYIW LRFEWQFAVG AILATTHDVV MTIGFFVITG
     IEFNLSSIAA ILTIVGYSLN DTVVVYDRIR ENLRRFKKMP MPQLLDLSMN QTLSRTIMTS
     VTTLLALIAL YAFGGEVIRS FTAAMIFGVL IGTYSSIFVA GPLLILFRLR PTGAAAKDAE
     ENGEEVAVKG
//
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