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Database: UniProt
Entry: U7VA69_9FUSO
LinkDB: U7VA69_9FUSO
Original site: U7VA69_9FUSO 
ID   U7VA69_9FUSO            Unreviewed;       312 AA.
AC   U7VA69;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-SEP-2017, entry version 21.
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=HMPREF0202_01420 {ECO:0000313|EMBL:ERT68612.1};
OS   Cetobacterium somerae ATCC BAA-474.
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae;
OC   Cetobacterium.
OX   NCBI_TaxID=1319815 {ECO:0000313|EMBL:ERT68612.1, ECO:0000313|Proteomes:UP000017081};
RN   [1] {ECO:0000313|EMBL:ERT68612.1, ECO:0000313|Proteomes:UP000017081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-474 {ECO:0000313|EMBL:ERT68612.1,
RC   ECO:0000313|Proteomes:UP000017081};
RA   Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R.,
RA   Fronick C., O'Laughlin M., Godfrey J., Miner T., Herter B.,
RA   Appelbaum E., Cordes M., Lek S., Wollam A., Pepin K.H., Palsikar V.B.,
RA   Mitreva M., Wilson R.K.;
RL   Submitted (AUG-2013) 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_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. 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:ERT68612.1}.
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DR   EMBL; AXZF01000054; ERT68612.1; -; Genomic_DNA.
DR   RefSeq; WP_023050958.1; NZ_KI518200.1.
DR   EnsemblBacteria; ERT68612; ERT68612; HMPREF0202_01420.
DR   PATRIC; fig|1319815.3.peg.1366; -.
DR   OrthoDB; POG091H02G4; -.
DR   Proteomes; UP000017081; 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; TIGR00916; 2A0604s01; 1.
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:SAAS00425060};
KW   Complete proteome {ECO:0000313|Proteomes:UP000017081};
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:UP000017081};
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     29       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    131    148       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    155    179       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    185    204       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    230    251       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    263    285       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   DOMAIN      155    284       SSD. {ECO:0000259|PROSITE:PS50156}.
SQ   SEQUENCE   312 AA;  34693 MW;  63000BBB9604761C CRC64;
     MYIEVIKHSK KWITLSTISF IIFLGMFLVK GLNYGIDFTG GSLIQLNYTN NITLTDINKE
     LDELAVEIPQ LSSTARKVQV SQADNNVIIR TAEMSDKETE KLLTNLQTLG DYKLERAEKV
     GATIGEELKT SAIYALTIGG LLIVLYITMR YEFKFAIAGI LTLLHDVTAA LGVIALLGYE
     VDTPFIAAIL TILGYSINDT IIIYDRIRES LRKKSDLTFG EVLNKSLNQV LVRSINTSVT
     TLLALVAILV FGGDSLRTFT TTLLVGIGVG TYSSIYISTP LVYLFEKKRD DKYEPKKDDD
     DDNSHPEEKI VV
//
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