GenomeNet

Database: UniProt
Entry: A0A0Q6L5L4_9SPHN
LinkDB: A0A0Q6L5L4_9SPHN
Original site: A0A0Q6L5L4_9SPHN 
ID   A0A0Q6L5L4_9SPHN        Unreviewed;       533 AA.
AC   A0A0Q6L5L4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-SEP-2017, entry version 10.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   ORFNames=ASG67_17050 {ECO:0000313|EMBL:KQU58039.1};
OS   Sphingomonas sp. Leaf339.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736343 {ECO:0000313|EMBL:KQU58039.1, ECO:0000313|Proteomes:UP000051371};
RN   [1] {ECO:0000313|EMBL:KQU58039.1, ECO:0000313|Proteomes:UP000051371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf339 {ECO:0000313|EMBL:KQU58039.1,
RC   ECO:0000313|Proteomes:UP000051371};
RA   Millard Andrew;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQU58039.1, ECO:0000313|Proteomes:UP000051371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf339 {ECO:0000313|EMBL:KQU58039.1,
RC   ECO:0000313|Proteomes:UP000051371};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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 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:KQU58039.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; LMRS01000005; KQU58039.1; -; Genomic_DNA.
DR   RefSeq; WP_056527119.1; NZ_LMRS01000005.1.
DR   EnsemblBacteria; KQU58039; KQU58039; ASG67_17050.
DR   Proteomes; UP000051371; 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; 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;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425060};
KW   Complete proteome {ECO:0000313|Proteomes:UP000051371};
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:UP000051371};
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    369    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    523       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
SQ   SEQUENCE   533 AA;  57435 MW;  E0D5CE7066705B6E CRC64;
     MLDFPRWKVW SIWALLAVLC ALAIPSVVPE RYTPTWLARA PRINLGLDLA GGSYLLLEAD
     VNDLAGTRIE TMRDQVQTEM RRGNPRIGIG DISTRDGQLS FLLRDPSQVD AARERLLTIT
     GGGAGMTGQR EWDIQVVDSS RFVLKPTEAG MTQAIDTAMN DATEVVRRRI DALGTREPTI
     IRQGTNRIVV QVPGLQNPQE LKDLLGKTAK LEFKLVDESA TPQQLAQRQA PIGSVILPYP
     SNPIGPPMIA LKRQTILSGD QIVDATQTFD PQTNAPQVAL TFNGPGGTRF ARVTQENTGK
     QFAIILDNSV ISAPNINEPI LGGRASISGN FTVDSANQLA IALRSGKLPI ALKVIEESTV
     GPELGADSIR AGVLASGVAV ALVVAFMLVT YGRFGFYANL AVVINVFVIL GVLALLKGTL
     TLPGIAGFVL TIGTAVDANV LINERIREER HRGRSVVQAV ELGYKEASRT IFEANVTHAI
     SGVIMLVLGS GPVKGFAVVL LIGICTSVFT AVTFTRMLVV LWIRRNKPKT INI
//
DBGET integrated database retrieval system