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Database: UniProt
Entry: A8ERU7_ARCB4
LinkDB: A8ERU7_ARCB4
Original site: A8ERU7_ARCB4 
ID   A8ERU7_ARCB4            Unreviewed;       322 AA.
AC   A8ERU7;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   28-FEB-2018, entry version 67.
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:ABV66671.1};
GN   OrderedLocusNames=Abu_0396 {ECO:0000313|EMBL:ABV66671.1};
OS   Arcobacter butzleri (strain RM4018).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Arcobacter.
OX   NCBI_TaxID=367737 {ECO:0000313|EMBL:ABV66671.1, ECO:0000313|Proteomes:UP000001136};
RN   [1] {ECO:0000313|EMBL:ABV66671.1, ECO:0000313|Proteomes:UP000001136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM4018 {ECO:0000313|EMBL:ABV66671.1,
RC   ECO:0000313|Proteomes:UP000001136};
RX   PubMed=18159241; DOI=10.1371/journal.pone.0001358;
RA   Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M.,
RA   Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G.,
RA   Malek J.A., Rogosin A., Stanker L.H., Mandrell R.E.;
RT   "The complete genome sequence and analysis of the
RT   Epsilonproteobacterium Arcobacter butzleri.";
RL   PLoS ONE 2:E1358-E1358(2007).
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 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}.
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; CP000361; ABV66671.1; -; Genomic_DNA.
DR   RefSeq; WP_012012225.1; NC_009850.1.
DR   ProteinModelPortal; A8ERU7; -.
DR   STRING; 367737.Abu_0396; -.
DR   EnsemblBacteria; ABV66671; ABV66671; Abu_0396.
DR   GeneID; 24305285; -.
DR   KEGG; abu:Abu_0396; -.
DR   eggNOG; ENOG4107RAB; Bacteria.
DR   eggNOG; COG0341; LUCA.
DR   HOGENOM; HOG000245914; -.
DR   KO; K03074; -.
DR   OMA; VNQTLMR; -.
DR   OrthoDB; POG091H02G4; -.
DR   BioCyc; ABUT367737:G1G6I-396-MONOMER; -.
DR   Proteomes; UP000001136; 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 inner membrane {ECO:0000256|HAMAP-Rule:MF_01464};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425060};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001136};
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:UP000001136};
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     17     35       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    136    153       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    159    181       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    239    261       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    267    289       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
SQ   SEQUENCE   322 AA;  36528 MW;  A7A75DD806004D1C CRC64;
     MEIFNQKKIY DFMGKKWPFL IFSTILMIIS LVLVFTRGFN FGIDFVGGTI VQVKYDQTAP
     IEKIREVLKD TKYASAVVTE FGSTEEVTIR ITGSSSDLTH DISDEMNKIL VPTGNFEIRK
     IDMVGSKVGA ELREKGVISL ILALAAILIY IGWRFEWRFA IASILGLIHD IIITLGLLSL
     FKVDINLDMI AAILTLVGYT INDTIIVNDR IREQVQITKE KDLDKIINES VSRTLSRTVL
     TSLSTLFVVT TMLIFGGEII YSFSFTLFVG IIIGTYSSIY FVSSFLKFFG FSVDDYRDKE
     AEKIKRKKDK EKLRSMYEQG TI
//
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