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Database: UniProt
Entry: A0A133XHI5_9RHOO
LinkDB: A0A133XHI5_9RHOO
Original site: A0A133XHI5_9RHOO 
ID   A0A133XHI5_9RHOO        Unreviewed;       625 AA.
AC   A0A133XHI5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-SEP-2017, entry version 11.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   ORFNames=AT959_13775 {ECO:0000313|EMBL:KXB30405.1};
OS   Dechloromonas denitrificans.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Azonexaceae; Dechloromonas.
OX   NCBI_TaxID=281362 {ECO:0000313|EMBL:KXB30405.1, ECO:0000313|Proteomes:UP000070186};
RN   [1] {ECO:0000313|EMBL:KXB30405.1, ECO:0000313|Proteomes:UP000070186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-841 {ECO:0000313|EMBL:KXB30405.1,
RC   ECO:0000313|Proteomes:UP000070186};
RA   Yoon S., Nissen S., Park D., Sanford R.A., Loeffler F.E.;
RT   "Nitrous oxide reduction kinetics distinguish bacteria harboring
RT   typical versus atypical NosZ.";
RL   Submitted (DEC-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:KXB30405.1}.
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DR   EMBL; LODL01000021; KXB30405.1; -; Genomic_DNA.
DR   RefSeq; WP_066883997.1; NZ_LODL01000021.1.
DR   EnsemblBacteria; KXB30405; KXB30405; AT959_13775.
DR   Proteomes; UP000070186; 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; 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 membrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425060};
KW   Complete proteome {ECO:0000313|Proteomes:UP000070186};
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:UP000070186};
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    448    467       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    472    492       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    498    518       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    539    565       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    571    595       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   DOMAIN        1    108       SecD-TM1. {ECO:0000259|Pfam:PF13721}.
SQ   SEQUENCE   625 AA;  67587 MW;  54DF63F7AAD5B0EA CRC64;
     MNRYPLWKYI TVAIALVLGF VYTLPNFFGE SPAVQVSSAK ATIKVDDKAR SRVEDALKTA
     GITHDGMQLD FNGVKTRFKD TDTQLKAKDV LEKAFNPDAS DPQYVVALNL LAASPQWLTS
     LHALPMYLGL DLRGGVHFLL QVDMKGALTK RLDSTSADLR TVLRDKNLRH AGVNREGDRL
     VVKFRDQETR DKARNAIADS QPDLILTEQA DGSEFKLVAT LKPEAQKRIG EFAIKQNITT
     LHNRINELGV AEPVIQQQGT DRIVVQLPGV QDTAKAKDIL GRTATLEIRM VDDSPGALEA
     ALAGNAPFGT EVYNERGGQP LLVKKQVVLT GDRLTDAQPG FDSQTQEAAV HLTLDSAGAR
     IFKDVTRENV NKRMAILLIE KGKGEVVTAP VIRTEIGGGR VQISGRMTTS EANDTALLLR
     AGSLAAPMDI VEERTIGPSL GADNIQKGFH STLWGFAAIA LFMIVYYQVF GVVSVLALGA
     NLLFLIALLS LLQATLTLPG IAAIALALGM AIDSNVLINE RVREELRNGM PPQAAISEGY
     ERAFGTILDS NVTTLIVGLM LLIFGSGPVR GFAVVHCLGI LTSIFSSVVV SRALINLIYG
     RQKKLAKVAI GQLWKPGTAT VNGQK
//
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