GSPG_ECOLI
ID GSPG_ECOLI Reviewed; 145 AA.
AC P41442; Q2M6Z3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Type II secretion system core protein G;
DE Short=T2SS core protein G;
DE AltName: Full=Protein transport protein HofG;
DE AltName: Full=Putative general secretion pathway protein G;
DE Flags: Precursor;
GN Name=gspG; Synonyms=hofG, hopG; OrderedLocusNames=b3328, JW3290;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [2]
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 [3]
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 [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).
CC -!- FUNCTION: Core component of the type II secretion system required for
CC the energy-dependent secretion of extracellular factors such as
CC proteases and toxins from the periplasm. Pseudopilin (pilin-like)
CC protein that polymerizes to form the pseudopilus. Further
CC polymerization triggers pseudopilus growth.
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. Forms
CC homomultimers. {ECO:0000250|UniProtKB:Q00514}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:Q00514}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Silenced by the DNA-binding protein H-NS under standard
CC growth conditions. {ECO:0000269|PubMed:11118204}.
CC -!- PTM: Cleaved by the prepilin peptidase. {ECO:0000250|UniProtKB:Q00514}.
CC -!- PTM: Methylated by prepilin peptidase at the amino group of the N-
CC terminal phenylalanine once the leader sequence is cleaved.
CC {ECO:0000250|UniProtKB:Q00514}.
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 G family. {ECO:0000305}.
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DR EMBL; U20786; AAA69031.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58125.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76353.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77963.1; -; Genomic_DNA.
DR PIR; B56150; B56150.
DR RefSeq; NP_417787.1; NC_000913.3.
DR RefSeq; WP_001202874.1; NZ_SSZK01000040.1.
DR AlphaFoldDB; P41442; -.
DR SMR; P41442; -.
DR BioGRID; 4262167; 250.
DR STRING; 511145.b3328; -.
DR PaxDb; P41442; -.
DR PRIDE; P41442; -.
DR EnsemblBacteria; AAC76353; AAC76353; b3328.
DR EnsemblBacteria; BAE77963; BAE77963; BAE77963.
DR GeneID; 947827; -.
DR KEGG; ecj:JW3290; -.
DR KEGG; eco:b3328; -.
DR PATRIC; fig|1411691.4.peg.3403; -.
DR EchoBASE; EB2723; -.
DR eggNOG; COG2165; Bacteria.
DR HOGENOM; CLU_091705_2_1_6; -.
DR InParanoid; P41442; -.
DR OMA; EMLVVIT; -.
DR PhylomeDB; P41442; -.
DR BioCyc; EcoCyc:G7706-MON; -.
DR BioCyc; MetaCyc:G7706-MON; -.
DR PRO; PR:P41442; -.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0015627; C:type II protein secretion system complex; IBA:GO_Central.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IBA:GO_Central.
DR InterPro; IPR000983; Bac_GSPG_pilin.
DR InterPro; IPR012902; N_methyl_site.
DR InterPro; IPR045584; Pilin-like.
DR InterPro; IPR013545; T2SS_protein-GspG_C.
DR InterPro; IPR010054; Type2_sec_GspG.
DR Pfam; PF07963; N_methyl; 1.
DR Pfam; PF08334; T2SSG; 1.
DR PRINTS; PR00813; BCTERIALGSPG.
DR SUPFAM; SSF54523; SSF54523; 1.
DR TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1.
DR TIGRFAMs; TIGR01710; typeII_sec_gspG; 1.
DR PROSITE; PS00409; PROKAR_NTER_METHYL; 1.
PE 2: Evidence at transcript level;
KW Cell inner membrane; Cell membrane; Membrane; Methylation;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT PROPEP 1..9
FT /note="Leader sequence"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT /id="PRO_0000449505"
FT CHAIN 10..145
FT /note="Type II secretion system core protein G"
FT /id="PRO_0000024201"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 123..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="N-methylphenylalanine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
SQ SEQUENCE 145 AA; 15905 MW; CBCD67D743810072 CRC64;
MRATDKQRGF TLLEIMVVIV IIGVLASLVV PNLMGNKEKA DKQKAVSDIV ALENALDMYK
LDNHHYPTTN QGLESLVEAP TLPPLAANYN KEGYIKRLPA DPWGNDYVLV NPGEHGAYDL
LSAGPDGEMG TEDDITNWGL SKKKK
