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Database: UniProt
Entry: A0A127JSY9_9BURK
LinkDB: A0A127JSY9_9BURK
Original site: A0A127JSY9_9BURK 
ID   A0A127JSY9_9BURK        Unreviewed;       317 AA.
AC   A0A127JSY9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-SEP-2017, entry version 8.
DE   RecName: Full=Protein-export membrane protein SecF {ECO:0000256|HAMAP-Rule:MF_01464};
GN   Name=secF {ECO:0000256|HAMAP-Rule:MF_01464};
GN   ORFNames=UC35_09580 {ECO:0000313|EMBL:AMO23097.1};
OS   Ramlibacter tataouinensis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Ramlibacter.
OX   NCBI_TaxID=94132 {ECO:0000313|EMBL:AMO23097.1, ECO:0000313|Proteomes:UP000070433};
RN   [1] {ECO:0000313|EMBL:AMO23097.1, ECO:0000313|Proteomes:UP000070433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5-10 {ECO:0000313|EMBL:AMO23097.1,
RC   ECO:0000313|Proteomes:UP000070433};
RX   PubMed=24425747; DOI=10.1099/ijs.0.058396-0;
RA   Lee H.J., Lee S.H., Lee S.S., Lee J.S., Kim Y., Kim S.C., Jeon C.O.;
RT   "Ramlibacter solisilvae sp. nov., isolated from forest soil, and
RT   emended description of the genus Ramlibacter.";
RL   Int. J. Syst. Evol. Microbiol. 64:1317-1322(2014).
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_01464, ECO:0000256|SAAS:SAAS00541769}.
CC   -!- SUBUNIT: Forms a complex with SecD. 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_01464}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01464}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01464}.
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01464}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01464}.
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DR   EMBL; CP010951; AMO23097.1; -; Genomic_DNA.
DR   RefSeq; WP_061498527.1; NZ_CP010951.1.
DR   EnsemblBacteria; AMO23097; AMO23097; UC35_09580.
DR   PATRIC; fig|94132.3.peg.1950; -.
DR   Proteomes; UP000070433; 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_01464_B; SecF_B; 1.
DR   InterPro; IPR022813; SecD/SecF_arch_bac.
DR   InterPro; IPR022645; SecD/SecF_bac.
DR   InterPro; IPR022646; SecD/SecF_CS.
DR   InterPro; IPR005665; SecF_bac.
DR   Pfam; PF07549; Sec_GG; 1.
DR   Pfam; PF02355; SecD_SecF; 1.
DR   PRINTS; PR01755; SECFTRNLCASE.
DR   TIGRFAMs; TIGR00916; 2A0604s01; 1.
DR   TIGRFAMs; TIGR00966; 3a0501s07; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425060};
KW   Complete proteome {ECO:0000313|Proteomes:UP000070433};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00284057};
KW   Protein transport {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425133};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070433};
KW   Translocation {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425069};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425065};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425143};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425109}.
FT   TRANSMEM     12     35       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    137    154       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    161    182       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    188    209       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    263    290       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
SQ   SEQUENCE   317 AA;  34934 MW;  8E477A249D346CB5 CRC64;
     MEFFKIRRDI PFMENALIFN VISFLTFAAA VFFLVTRGLH LSVEFTGGTV MEVGYSQPAD
     VERVRRTVAG LGFADVQVQN FGTSRDVLIR LPAQKGVSSA QQSEKVLSAL KAEDPGVTLR
     RTEFVGPQVG EELATDGLKA LAMVVIGIMV YLAFRFEWKF AVAAIVANLH DVVIILGFFA
     YFQWEFSLAV LAAVLAVLGY SVNESVVIFD RIRENFRRYR KMNTVQIIDN AITSTISRTI
     ITHGSTQIMV LSMLLFGGPT LHYFALALTI GILFGIYSSV FVAAAIAMWL GIKREDLVKS
     SGRKEEDPND PNAGAAV
//
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