GSPF_ECOLI
ID GSPF_ECOLI Reviewed; 398 AA.
AC P41441; Q2M6Z2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Putative type II secretion system protein F;
DE Short=T2SS protein F;
DE AltName: Full=General secretion pathway protein F;
DE AltName: Full=Protein transport protein HofF;
GN Name=gspF; Synonyms=hofF, hopF; OrderedLocusNames=b3327, JW3289;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 195-398.
RC STRAIN=K12;
RX PubMed=7896718; DOI=10.1128/jb.177.7.1892-1895.1995;
RA Stojiljkovic I., Schoenherr R., Kusters J.G.;
RT "Identification of the hopG gene, a component of Escherichia coli K-12 type
RT II export system, and its conservation among different pathogenic
RT Escherichia coli and Shigella isolates.";
RL J. Bacteriol. 177:1892-1895(1995).
RN [4]
RP LACK OF EXPRESSION, AND GENE NAME.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8655552; DOI=10.1128/jb.178.12.3544-3549.1996;
RA Francetic O., Pugsley A.P.;
RT "The cryptic general secretory pathway (gsp) operon of Escherichia coli K-
RT 12 encodes functional proteins.";
RL J. Bacteriol. 178:3544-3549(1996).
RN [5]
RP LACK OF EXPRESSION, AND TRANSCRIPTIONAL REGULATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11118204; DOI=10.1093/emboj/19.24.6697;
RA Francetic O., Belin D., Badaut C., Pugsley A.P.;
RT "Expression of the endogenous type II secretion pathway in Escherichia coli
RT leads to chitinase secretion.";
RL EMBO J. 19:6697-6703(2000).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Component of the type II secretion system inner membrane
CC complex required for the energy-dependent secretion of extracellular
CC factors such as proteases and toxins from the periplasm.
CC {ECO:0000250|UniProtKB:Q00514}.
CC -!- SUBUNIT: Type II secretion system is composed of four main components:
CC the outer membrane complex, the inner membrane complex, the cytoplasmic
CC secretion ATPase and the periplasm-spanning pseudopilus (By
CC similarity). Homodimer (By similarity). Interacts with GspE and GspL
CC components (By similarity). {ECO:0000250|UniProtKB:P45780,
CC ECO:0000250|UniProtKB:Q00513, ECO:0000250|UniProtKB:Q00514}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- INDUCTION: Silenced by the DNA-binding protein H-NS under standard
CC growth conditions. {ECO:0000269|PubMed:11118204}.
CC -!- MISCELLANEOUS: Part of a cryptic operon that encodes proteins involved
CC in type II secretion machinery in other organisms, but is not expressed
CC in strain K12.
CC -!- SIMILARITY: Belongs to the GSP F family. {ECO:0000305}.
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DR EMBL; U18997; AAA58124.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76352.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77964.1; -; Genomic_DNA.
DR EMBL; U20786; AAA69030.1; -; Genomic_DNA.
DR PIR; B65126; B65126.
DR RefSeq; NP_417786.1; NC_000913.3.
DR RefSeq; WP_001109573.1; NZ_STEB01000038.1.
DR AlphaFoldDB; P41441; -.
DR SMR; P41441; -.
DR BioGRID; 4262168; 120.
DR STRING; 511145.b3327; -.
DR PaxDb; P41441; -.
DR PRIDE; P41441; -.
DR EnsemblBacteria; AAC76352; AAC76352; b3327.
DR EnsemblBacteria; BAE77964; BAE77964; BAE77964.
DR GeneID; 947829; -.
DR KEGG; ecj:JW3289; -.
DR KEGG; eco:b3327; -.
DR PATRIC; fig|1411691.4.peg.3404; -.
DR EchoBASE; EB2722; -.
DR eggNOG; COG1459; Bacteria.
DR HOGENOM; CLU_035032_0_1_6; -.
DR InParanoid; P41441; -.
DR OMA; FSRQMYS; -.
DR PhylomeDB; P41441; -.
DR BioCyc; EcoCyc:G7705-MON; -.
DR BioCyc; MetaCyc:G7705-MON; -.
DR PRO; PR:P41441; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015627; C:type II protein secretion system complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IBA:GO_Central.
DR Gene3D; 1.20.81.30; -; 2.
DR InterPro; IPR003004; GspF/PilC.
DR InterPro; IPR011850; T2SS_GspF.
DR InterPro; IPR001992; T2SS_GspF/T4SS_PilC_CS.
DR InterPro; IPR018076; T2SS_GspF_dom.
DR InterPro; IPR042094; T2SS_GspF_sf.
DR PANTHER; PTHR30012; PTHR30012; 1.
DR Pfam; PF00482; T2SSF; 2.
DR PRINTS; PR00812; BCTERIALGSPF.
DR TIGRFAMs; TIGR02120; GspF; 1.
DR PROSITE; PS00874; T2SP_F; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell inner membrane; Cell membrane; Membrane; Metal-binding;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..398
FT /note="Putative type II secretion system protein F"
FT /id="PRO_0000207831"
FT TOPO_DOM 1..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00513"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..216
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00513"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00513"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..398
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT BINDING 90
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P45780"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P45780"
FT BINDING 148
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P45780"
FT CONFLICT 270
FT /note="T -> P (in Ref. 3; AAA69030)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 44339 MW; 8A2696AC7948BC8A CRC64;
MNYRYRAMTQ DGQKLQGIID ANDERQARLR LREEGLFLLD IRPQKSSGVK TRRPRISHSE
LTLFTRQLAT LSAAALPLEE SLAVIGQQSS NKRLGDVLNQ VRSAILEGHP LSDALQHFPT
LFDSLYRTLV KAGEKSGLLA PVLEKLADYN ENRQKIRSKL IQSLIYPCML TTVAIGVVII
LLTAVVPKIT EQFVHMKQQL PLSTRILLGL SDTLQRTGPT LLATVFIVAV GFWLWLKRGN
NRHRFHAMLL RVALIGPLIC AINSARYLRT LSILQSSGVP LLDGMNLSTE SLNNLEIRQR
LANAAENVRQ GNSIHLSLEQ TAIFPPMMLY MVASGEKSGQ LGTLMVRAAD NQETLQQNRI
ALTLSIFEPA LIITMALIVL FIVVSVLQPL LQLNSMIN
