(data stored in ACNUC7421 zone)

SWISSPROT: D4YYJ0_SPHJU

ID   D4YYJ0_SPHJU            Unreviewed;       533 AA.
AC   D4YYJ0;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 46.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463,
GN   ECO:0000313|EMBL:BAI95422.1};
GN   OrderedLocusNames=SJA_C1-05880 {ECO:0000313|EMBL:BAI95422.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95422.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95422.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
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 inner 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; AP010803; BAI95422.1; -; Genomic_DNA.
DR   RefSeq; WP_013039141.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-05880; -.
DR   EnsemblBacteria; BAI95422; BAI95422; SJA_C1-05880.
DR   GeneID; 29272264; -.
DR   KEGG; sjp:SJA_C1-05880; -.
DR   eggNOG; ENOG4107QN8; Bacteria.
DR   eggNOG; COG0342; LUCA.
DR   HOGENOM; HOG000018636; -.
DR   KO; K03072; -.
DR   OMA; AAPMEII; -.
DR   OrthoDB; POG091H02C5; -.
DR   Proteomes; UP000007753; Chromosome 1.
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-HAMAP.
DR   GO; GO:0006605; P:protein targeting; IEA:UniProtKB-HAMAP.
DR   GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_01463_B; SecD_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   Pfam; PF07549; Sec_GG; 1.
DR   Pfam; PF02355; SecD_SecF; 1.
DR   TIGRFAMs; TIGR00916; 2A0604s01; 1.
DR   TIGRFAMs; TIGR01129; secD; 1.
PE   3: Inferred from homology;
DR   PRODOM; D4YYJ0.
DR   SWISS-2DPAGE; D4YYJ0.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01463};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425060};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
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:UP000007753};
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    371    389       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    396    416       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    422    442       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    471    490       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    496    519       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
SQ   SEQUENCE   533 AA;  56698 MW;  6A9855CE604B9FD7 CRC64;
     MLNFPRWAVV AILLPLLIGI ACAVPSFLPD SVVGQLPKFM QTRVNLGLDL SGGSHLLLEA
     STQDVAKQRI ANMEEQVRTE LRRGDTKIAI GDISSRDGKL SFMVRNPSQV DAAVERIRPL
     TQGAGLTGQR DFNVEVVNSS TIVITPTKAG IDNAVKGAME VATEVIRKRI DEMGTREPTI
     QQQGDNRIVV QVPGLQDPKA LKDLLGQTAK LEFKLVDVNA NPAEVAQGRA PVGSEVLPYP
     TNPAGPPVIA VYRQVMVSGE DLTDAQQGYD QTGNQPIVNI RFNGAGGRKF GQVTSQNVNR
     PFAIILDGQV LSAPNINEPI LGGSAQISGS FTVESANQLA IALRSGKLPV ALTVVEERTV
     GPQLGADSIR AGLMASVIAV AAVAAFMFVS YGRFGMYANL AVAINVLVIL GVMGILGATL
     TLPGIAGFVL TIGTAVDANV LIYERIREER RRGRGVVQAI EHGYKEASRT IFEANVTHAI
     AGGIMLALGS GPVKGFAIVL LIGIATSVFT AVTFTRLLVS RWVRAKRPTE IHI
//

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