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Database: UniProt
Entry: C0R170_BRAHW
LinkDB: C0R170_BRAHW
Original site: C0R170_BRAHW 
ID   C0R170_BRAHW            Unreviewed;       307 AA.
AC   C0R170;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-SEP-2017, entry version 59.
DE   RecName: Full=Protein-export membrane protein SecF {ECO:0000256|HAMAP-Rule:MF_01464};
GN   Name=secF {ECO:0000256|HAMAP-Rule:MF_01464,
GN   ECO:0000313|EMBL:ACN83858.1};
GN   OrderedLocusNames=BHWA1_01382 {ECO:0000313|EMBL:ACN83858.1};
OS   Brachyspira hyodysenteriae (strain ATCC 49526 / WA1).
OC   Bacteria; Spirochaetes; Brachyspirales; Brachyspiraceae; Brachyspira.
OX   NCBI_TaxID=565034 {ECO:0000313|EMBL:ACN83858.1, ECO:0000313|Proteomes:UP000001803};
RN   [1] {ECO:0000313|EMBL:ACN83858.1, ECO:0000313|Proteomes:UP000001803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49526 / WA1 {ECO:0000313|Proteomes:UP000001803}, and WA1
RC   {ECO:0000313|EMBL:ACN83858.1};
RX   PubMed=19262690; DOI=10.1371/journal.pone.0004641;
RA   Bellgard M.I., Wanchanthuek P., La T., Ryan K., Moolhuijzen P.,
RA   Albertyn Z., Shaban B., Motro Y., Dunn D.S., Schibeci D., Hunter A.,
RA   Barrero R., Phillips N.D., Hampson D.J.;
RT   "Genome sequence of the pathogenic intestinal spirochete Brachyspira
RT   hyodysenteriae reveals adaptations to its lifestyle in the porcine
RT   large intestine.";
RL   PLoS ONE 4:E4641-E4641(2009).
RN   [2] {ECO:0000313|EMBL:ACD74831.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WA1 {ECO:0000313|EMBL:ACD74831.1};
RX   PubMed=19179021; DOI=10.1016/j.vetmic.2008.12.018;
RA   Song Y., La T., Phillips N.D., Bellgard M.I., Hampson D.J.;
RT   "A reverse vaccinology approach to swine dysentery vaccine
RT   development.";
RL   Vet. Microbiol. 137:111-119(2009).
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 inner 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}.
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DR   EMBL; EU555161; ACD74831.1; -; Genomic_DNA.
DR   EMBL; CP001357; ACN83858.1; -; Genomic_DNA.
DR   RefSeq; WP_012670903.1; NC_012225.1.
DR   STRING; 565034.BHWA1_01382; -.
DR   EnsemblBacteria; ACN83858; ACN83858; BHWA1_01382.
DR   GeneID; 31722560; -.
DR   KEGG; bhy:BHWA1_01382; -.
DR   eggNOG; ENOG4107XHD; Bacteria.
DR   eggNOG; COG0341; LUCA.
DR   HOGENOM; HOG000245914; -.
DR   KO; K03074; -.
DR   OMA; VNQTLMR; -.
DR   OrthoDB; POG091H02G4; -.
DR   Proteomes; UP000001803; 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; TIGR00966; 3a0501s07; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01464};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00018194};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001803};
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:UP000001803};
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     20     42       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    149    167       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    174    195       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    201    225       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    246    270       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    276    301       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   NON_TER     307    307       {ECO:0000313|EMBL:ACD74831.1}.
SQ   SEQUENCE   307 AA;  34298 MW;  5B95A5A7C22E0576 CRC64;
     MSEEIKKENN DLTKNKIPFV KIMPIAAVVS SILFIASIAL FVNKLTTNSF NMGIDFAGGV
     ELKVQIDNPE VINIAEIRAL YNNFGTETVN IQELEGADNV NAFLLRFRGS NEESDRAMQV
     LYDKYTQEKV NLIGSNIISG VVSADNLKLA FILIIVSWII IMIYITIRFN YRYAFPAIIT
     LIHNVVIVFG ILLFLNKEFS VLVLSSMLTL IGYTINDIIV VFDRIRENAN SKKPFKEIVN
     ISLNNVVGRT IITSISTLLA ALAIMIWGGF ILYDFAFTFF CGVVIGTYAS NFIASGLLIL
     FMKTKKA
//
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