Back to PBIL home page
ID D4YYJ0_SPHJU Unreviewed; 533 AA.
AC D4YYJ0;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 16-JAN-2019, entry version 52.
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 DSM 16413 / CCM 7287 / MTCC 6362 / UT26
OS / 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=DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S
RC {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:SAAS01082309}.
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}.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC -----------------------------------------------------------------------
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 Proteomes; UP000007753; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IPR022813; SecD/SecF_arch_bac.
DR InterPro; IPR022645; SecD/SecF_bac.
DR InterPro; IPR022646; SecD/SecF_CS.
DR PANTHER; PTHR30081; PTHR30081; 1.
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:SAAS01082273}; Coiled coil {ECO:0000256|SAM:Coils};
KW Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW ECO:0000256|SAAS:SAAS01082292};
KW Protein transport {ECO:0000256|HAMAP-Rule:MF_01463,
KW ECO:0000256|SAAS:SAAS01082319};
KW Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW Translocation {ECO:0000256|HAMAP-Rule:MF_01463,
KW ECO:0000256|SAAS:SAAS01082267};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW ECO:0000256|SAAS:SAAS01082280};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01463,
KW ECO:0000256|SAAS:SAAS01082333};
KW Transport {ECO:0000256|HAMAP-Rule:MF_01463,
KW ECO:0000256|SAAS:SAAS01082300}.
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}.
FT COILED 63 83 {ECO:0000256|SAM:Coils}.
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
//
Back to PBIL home page