ID   A8TKV2_9PROT            Unreviewed;       317 AA.
AC   A8TKV2;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   21-MAR-2012, entry version 18.
DE   RecName: Full=Protein translocase subunit SecF;
GN   Name=secF; ORFNames=BAL199_25189;
OS   alpha proteobacterium BAL199.
OC   Bacteria; Proteobacteria; Alphaproteobacteria.
OX   NCBI_TaxID=331869;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BAL199;
RA   Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA   Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (OCT-2007) 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 (By similarity).
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 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data.
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DR   EMBL; ABHC01000002; EDP66303.1; -; Genomic_DNA.
DR   ProteinModelPortal; A8TKV2; -.
DR   PATRIC; 30873868; VBIAlpPro7182_0931.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
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:HAMAP.
DR   GO; GO:0006605; P:protein targeting; IEA:HAMAP.
DR   GO; GO:0043952; P:protein transport by the Sec complex; IEA:HAMAP.
DR   HAMAP; MF_01464_B; SecF_B; 1; -.
DR   InterPro; IPR022813; SecD/SecF.
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; Membrane; Protein transport; Translocation;
KW   Transmembrane; Transmembrane helix; Transport.
FT   TRANSMEM     21     41       Helical; (By similarity).
FT   TRANSMEM    137    157       Helical; (By similarity).
FT   TRANSMEM    165    185       Helical; (By similarity).
FT   TRANSMEM    191    211       Helical; (By similarity).
FT   TRANSMEM    243    265       Helical; (By similarity).
FT   TRANSMEM    269    291       Helical; (By similarity).
SQ   SEQUENCE   317 AA;  34667 MW;  C386EE43566D89B7 CRC64;
     MLKPIRFVPR NPKLPIIKSR LAAFVFSALL ILGSLTAVAT IGLNFGIDFK GGILMEVRTP
     GVADISAMRS TLNGLDLGDV SLQEFGDERE VLIRIQRQSG DEAAQIKATE AVRVALGEGV
     EFRRTEFVGP TVGQELIEAG VLAVGLALLS ILFYVWFRFE WQFGVGALVA LAHDIISTMG
     LFAIIQHEFN LATVAAVLTI AGYSINDTVV IYDRVRENLR KYKKMPLADL FELSVNETLS
     RTTLTSGTTL LALFAIYLFG GAVLADFALA MIWGIVIGTY SSILIAVPLL LYTGVRRGDD
     HLDPSQVPEY ERAERES
//