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Database: UniProt
Entry: A0A0G1Q827_9BACT
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ID   A0A0G1Q827_9BACT        Unreviewed;       323 AA.
AC   A0A0G1Q827;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-SEP-2017, entry version 11.
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=UX07_C0028G0006 {ECO:0000313|EMBL:KKU04740.1};
OS   Parcubacteria group bacterium GW2011_GWA2_45_30.
OC   Bacteria; unclassified Parcubacteria group.
OX   NCBI_TaxID=1618834 {ECO:0000313|EMBL:KKU04740.1, ECO:0000313|Proteomes:UP000033829};
RN   [1] {ECO:0000313|EMBL:KKU04740.1, ECO:0000313|Proteomes:UP000033829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a
RT   large radiation of phyla.";
RL   Nature 0:0-0(2015).
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:SAAS00541936}.
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. Other proteins may also be involved.
CC       {ECO:0000256|HAMAP-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: 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:KKU04740.1}.
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DR   EMBL; LCKU01000028; KKU04740.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKU04740; KKU04740; UX07_C0028G0006.
DR   PATRIC; fig|1618834.3.peg.603; -.
DR   Proteomes; UP000033829; 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_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   InterPro; IPR000731; SSD.
DR   Pfam; PF07549; Sec_GG; 1.
DR   Pfam; PF02355; SecD_SecF; 1.
DR   PRINTS; PR01755; SECFTRNLCASE.
DR   TIGRFAMs; TIGR00966; 3a0501s07; 1.
DR   PROSITE; PS50156; SSD; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00018194};
KW   Complete proteome {ECO:0000313|Proteomes:UP000033829};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00018303};
KW   Protein transport {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00018248};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033829};
KW   Translocation {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00018306};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00018265};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00018174};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425232}.
FT   TRANSMEM     24     45       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    150    169       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    181    207       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    213    234       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    266    283       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    289    316       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   DOMAIN      150    315       SSD. {ECO:0000259|PROSITE:PS50156}.
SQ   SEQUENCE   323 AA;  35384 MW;  022565C996B35C65 CRC64;
     MSQAKISHLS YISNGMNIIG NKNIFLTISG ILVLGSLISI AVWGLKFGID FTGGSLLEVE
     FIAVRPDAAK IRQSLEPFSI GNITVQPTGE RGMILRFAHV DEGKHQQILE VLSKIESAGQ
     GVESEKQIAV IAKRFDTIGP TIGRELYRNS LIALGVAIVA IILYIAFAFR HVSKPVSSWK
     YGVSAVIALI HDVTIPAGIF AVLGNFWGIE VDTLFITALL TILGFSVHDT IVVFDRIREN
     LRKLKQPEPF EITVNRSVNE TIARSINTSL TVLLVLVAIM AFGGVTTRYF ALALIFGIVF
     GTYSSIFVAS PILVIWQRLT RKI
//
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