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Database: UniProt
Entry: I0HLA8_RUBGI
LinkDB: I0HLA8_RUBGI
Original site: I0HLA8_RUBGI 
ID   I0HLA8_RUBGI            Unreviewed;       635 AA.
AC   I0HLA8;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   28-FEB-2018, entry version 30.
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:BAL93795.1};
GN   OrderedLocusNames=RGE_04500 {ECO:0000313|EMBL:BAL93795.1};
OS   Rubrivivax gelatinosus (strain NBRC 100245 / IL144).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Rubrivivax.
OX   NCBI_TaxID=983917 {ECO:0000313|EMBL:BAL93795.1, ECO:0000313|Proteomes:UP000007883};
RN   [1] {ECO:0000313|EMBL:BAL93795.1, ECO:0000313|Proteomes:UP000007883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100245 / IL144 {ECO:0000313|Proteomes:UP000007883};
RX   PubMed=22689232; DOI=10.1128/JB.00511-12;
RA   Nagashima S., Kamimura A., Shimizu T., Nakamura-isaki S., Aono E.,
RA   Sakamoto K., Ichikawa N., Nakazawa H., Sekine M., Yamazaki S.,
RA   Fujita N., Shimada K., Hanada S., Nagashima K.V.P.;
RT   "Complete genome sequence of phototrophic betaproteobacterium
RT   Rubrivivax gelatinosus IL144.";
RL   J. Bacteriol. 194:3541-3542(2012).
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; AP012320; BAL93795.1; -; Genomic_DNA.
DR   RefSeq; WP_014426671.1; NC_017075.1.
DR   EnsemblBacteria; BAL93795; BAL93795; RGE_04500.
DR   KEGG; rge:RGE_04500; -.
DR   PATRIC; fig|983917.3.peg.442; -.
DR   KO; K03072; -.
DR   OMA; AAPMEII; -.
DR   OrthoDB; POG091H02C5; -.
DR   BioCyc; RGEL983917:G1H8K-443-MONOMER; -.
DR   Proteomes; UP000007883; Chromosome.
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; IPR027398; SecD-TM.
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; PF13721; SecD-TM1; 1.
DR   Pfam; PF02355; SecD_SecF; 1.
DR   TIGRFAMs; TIGR00916; 2A0604s01; 1.
DR   TIGRFAMs; TIGR01129; secD; 1.
PE   3: Inferred from homology;
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:UP000007883};
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:UP000007883};
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    455    472       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    574    598       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   DOMAIN        1    107       SecD-TM1. {ECO:0000259|Pfam:PF13721}.
SQ   SEQUENCE   635 AA;  68773 MW;  C6F77CB8A10EC1E8 CRC64;
     MNRYPWWKYA ILAFAFVVGL LYTVPNFYGE APAVQVSSGK ATVKMDPAMV QRVEQILSSA
     GLKADFVQLD GTSVRARFDD TDTQIKAKDA IAHALNPDAN DPTWIVALNL VSRSPQWMAR
     IHALPMYLGL DLRGGVHFLM QVDMKAALTK KAEAVAGDVR TLLRDKNIRH AGITREGNAV
     EVRFRETALA EQARSLLTDQ LPDLQWTPTA DAATGDTKLV GTLKPQAATR VQEQALKQNI
     STLNNRVNEL GVAEPVIQQQ GIDRVVVQLP GVQDTAKAKD IIGRTATLEI RLVNETNEAM
     DAVRGSGPVP FGSERFLERG GQPVIVYRNV VLTGENLTDA QPGFDGQTHE PTVNLTLDAR
     GARIFKDVTR ENVGKRMAIL LFEKGKGEVV TAPVIRSEIG GGRVQISGRM TTEEASDQAL
     LLRAGSLAAP MEIIEERTIG PSLGAENIAK GFHSVLWGFV AIAIFMCLYY MLFGVFSTLA
     LAFNLLMLIA VLSMLQATLS LPGIAAIALV LGMAIDSNVL INERVREELR HGATPQVAIN
     AGYERAFGTI LDSNVTTLIA GLALLAFGSG PVRGFAVVHC LGILTSMFSS VMFSRGLVNL
     WYGRQKKLKS VSIGQVWRPD GGTPVPAEDK QNAKA
//
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