(data stored in SCRATCH zone)

SWISSPROT: B7UJN2_ECO27

ID   B7UJN2_ECO27            Unreviewed;       323 AA.
AC   B7UJN2;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, 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:CAS07892.1};
GN   OrderedLocusNames=E2348C_0344 {ECO:0000313|EMBL:CAS07892.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07892.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07892.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(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:SAAS01082309}.
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}.
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DR   EMBL; FM180568; CAS07892.1; -; Genomic_DNA.
DR   RefSeq; WP_000046637.1; NC_011601.1.
DR   SMR; B7UJN2; -.
DR   EnsemblBacteria; CAS07892; CAS07892; E2348C_0344.
DR   KEGG; ecg:E2348C_0344; -.
DR   HOGENOM; HOG000245914; -.
DR   KO; K03074; -.
DR   OMA; VNQTLMR; -.
DR   BioCyc; ECOL574521:E2348C_RS01810-MONOMER; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0016021; C:integral component of 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: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   PANTHER; PTHR30081; PTHR30081; 1.
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;
DR   PRODOM; B7UJN2.
DR   SWISS-2DPAGE; B7UJN2.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01464};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS01082273};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS01082292};
KW   Protein transport {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS01082319};
KW   Translocation {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS01082267};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS01082280};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS01082333};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS01082300}.
FT   TRANSMEM     24     43       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    142    163       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    170    191       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    197    217       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    248    266       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    272    297       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
SQ   SEQUENCE   323 AA;  35382 MW;  9662196085448643 CRC64;
     MAQEYTVEQL NHGRKVYDFM RWDYWAFGIS GLLLIAAIVI MGVRGFNWGL DFTGGTVIEI
     TLEKPAEIDV MRDALQKAGF EEPMLQNFGS SHDIMVRMPP AEGETGGQVL GSQVLKVINE
     STNQNAAVKR IEFVGPSVGA DLAQTGAMAL MAALLSILVY VGFRFEWRLA AGVVIALAHD
     VIITLGILSL FHIEIDLTIV ASLMSVIGYS LNDSIVVSDR IRENFRKIRR GTPYEIFNVS
     LTQTLHRTLI TSGTTLMVIL MLYLFGGPVL EGFSLTMLIG VSIGTASSIY VASALALKLG
     MKREHMLQQK VEKEGADQPS ILP
//

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