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Database: UniProt
Entry: W4P9H5_9BACE
LinkDB: W4P9H5_9BACE
Original site: W4P9H5_9BACE 
ID   W4P9H5_9BACE            Unreviewed;       995 AA.
AC   W4P9H5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   23-MAY-2018, entry version 27.
DE   SubName: Full=Protein-export membrane protein SecD {ECO:0000313|EMBL:GAE16390.1};
GN   Name=secF {ECO:0000256|HAMAP-Rule:MF_01464};
GN   Synonyms=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   ORFNames=JCM6292_2810 {ECO:0000313|EMBL:GAE16390.1};
OS   Bacteroides pyogenes JCM 6292.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1235809 {ECO:0000313|EMBL:GAE16390.1, ECO:0000313|Proteomes:UP000018861};
RN   [1] {ECO:0000313|EMBL:GAE16390.1, ECO:0000313|Proteomes:UP000018861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 6292 {ECO:0000313|EMBL:GAE16390.1,
RC   ECO:0000313|Proteomes:UP000018861};
RA   Sakamoto M., Oshima K., Suda W., Kitamura K., Iida T., Hattori M.,
RA   Ohkuma M.;
RT   "Draft Genome Sequences of Three Strains of Bacteroides pyogenes
RT   Isolated from a Cat and Swine.";
RL   Genome Announc. 2:e01242-13(2014).
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_01464, 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. Other proteins may also be involved.
CC       {ECO:0000256|HAMAP-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. Other proteins may also be involved.
CC       {ECO:0000256|HAMAP-Rule:MF_01463}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01464}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01464}.
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_01464}.
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:GAE16390.1}.
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DR   EMBL; BAIQ01000033; GAE16390.1; -; Genomic_DNA.
DR   RefSeq; WP_027325686.1; NZ_BAIQ01000033.1.
DR   EnsemblBacteria; GAE16390; GAE16390; JCM6292_2810.
DR   Proteomes; UP000018861; 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; 1.
DR   TIGRFAMs; TIGR00966; 3a0501s07; 1.
DR   TIGRFAMs; TIGR01129; secD; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425060};
KW   Complete proteome {ECO:0000313|Proteomes:UP000018861};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00284057};
KW   Protein transport {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425133};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018861};
KW   Translocation {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425069};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425065};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425143};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425109}.
FT   TRANSMEM    503    524       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    531    550       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    556    574       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    595    620       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    626    650       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    687    707       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    825    843       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    855    876       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    882    899       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    931    954       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    960    984       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
SQ   SEQUENCE   995 AA;  109448 MW;  C163A9B486ED0EF6 CRC64;
     MQNKGLVKVF AVALTLVCAF YLSFSFVTRH YTKKAKEIAK GDPKVEQDYL DSLSNERVWL
     GNWTLKDCRE MEISLGLDLK GGMNVILEVS VPDVIKALAD NKPDEAFNKA LSEAAKQAIN
     SQEDVISLFV KEYRKIAPGA KLSELFATQQ LKDKVNQKST DAEVEKVLRE EVKAAVENSY
     NVLRTRIDRF GVVQPNIQSL EDKMGRIMVE LPGIKEPERV RKLLQGSANL EFWETYTARE
     LLSYMQAADS KLRSLLAQDT EESVADTTAA EQTEAVKKTV SAADSLAAAL KGDAKEDKEA
     DLKEFKKQYP LLAILQLNSS GQGPVIGYAN YKDTAEVNKY LSMDEIKAQL PKDLRLKWGV
     SPAEFDKKGQ IFELYAIKST ERNGRAPLEG DVVTDAKDEY DQFGKPAVSM GMNADGARRW
     AQLTKQNIGR SIAIVLDNYV YSAPNVYSEI TGGRSQITGH FTPEQAKDLA NVLKSGKMPA
     PARIVQEDIV GPSLGQESIN AGIISFVIAL VLLMIYMCAM YGFIPGMVAN GALFLNFFFT
     LGILSSFQAA LTMSGIAGMV LSLGMAVDAN VLIYERTKEE LRSGKGLQKA LADGYSNAFS
     AIFDSNLTSI ITGIILFNFG TGPIRGFATT LIIGILVSFF TAVFMTRLVY EHFMAKDKWL
     NLTFSTGISK NLMANTRFDF MGAGKKALII AGVFILICFG SFAIRGLSQS IDFTGGRNFK
     VQFENPVQPE QIRELISSKF GDSNVSVIAV GTDKKTVRIS TNYRIDDNSE TVDSEIEAYL
     YETLKPVLTQ NITLDTFIDR DNYTGGSIVS SQKVGPSIAD DIKTGAIYSV VLALIAIGLY
     ILLRFRNIAY SVGSVVALTS DTIMIIGFYS LLWGVVPFSL EIDQTFIGAI LTAIGYSIND
     KVVIFDRVRE FFGLYPKRSE RQLFNDSLNT TLARTINTSL STLIVLLCIF ILGGDSIRSF
     AFAMILGVVI GTMSSLFIAS PIAYSMLKGK KRGED
//
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