GSPH_ECOLI
ID GSPH_ECOLI Reviewed; 169 AA.
AC P41443; Q2M6Z4;
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 protein H;
DE Short=T2SS minor pseudopilin H;
DE AltName: Full=General secretion pathway protein H;
DE AltName: Full=Protein transport protein HofH;
DE AltName: Full=Putative general secretion pathway protein H;
DE Flags: Precursor;
GN Name=gspH; Synonyms=hofH, hopH; OrderedLocusNames=b3329, JW3291;
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 1-30.
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).
CC -!- FUNCTION: Component of the type II secretion system required for the
CC energy-dependent secretion of extracellular factors such as proteases
CC and toxins from the periplasm. Part of the pseudopilus tip complex that
CC is critical for the recognition and binding of secretion substrates.
CC {ECO:0000250|UniProtKB:Q00515}.
CC -!- SUBUNIT: Type II secretion is composed of four main components: the
CC outer membrane complex, the inner membrane complex, the cytoplasmic
CC secretion ATPase and the periplasm-spanning pseudopilus. Interacts with
CC core component GspG. {ECO:0000250|UniProtKB:Q00515}.
CC -!- INTERACTION:
CC P41443; P76086: paaX; NbExp=2; IntAct=EBI-1129978, EBI-544692;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:Q00515}; 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 prepilin peptidase. {ECO:0000250|UniProtKB:Q00515}.
CC -!- PTM: Methylated by prepilin peptidase at the amino group of the N-
CC terminal phenylalanine once the leader sequence is cleaved by prepilin
CC peptidase. {ECO:0000250|UniProtKB:Q00515}.
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 H family. {ECO:0000305}.
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DR EMBL; U18997; AAA58126.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76354.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77962.1; -; Genomic_DNA.
DR EMBL; U20786; AAA69032.1; -; Genomic_DNA.
DR PIR; D65126; D65126.
DR RefSeq; NP_417788.1; NC_000913.3.
DR RefSeq; WP_001076046.1; NZ_SSZK01000040.1.
DR PDB; 2KNQ; NMR; -; A=30-169.
DR PDBsum; 2KNQ; -.
DR AlphaFoldDB; P41443; -.
DR SMR; P41443; -.
DR BioGRID; 4262246; 206.
DR BioGRID; 852146; 3.
DR IntAct; P41443; 4.
DR STRING; 511145.b3329; -.
DR PaxDb; P41443; -.
DR PRIDE; P41443; -.
DR DNASU; 947834; -.
DR EnsemblBacteria; AAC76354; AAC76354; b3329.
DR EnsemblBacteria; BAE77962; BAE77962; BAE77962.
DR GeneID; 947834; -.
DR KEGG; ecj:JW3291; -.
DR KEGG; eco:b3329; -.
DR PATRIC; fig|1411691.4.peg.3402; -.
DR EchoBASE; EB2724; -.
DR eggNOG; COG2165; Bacteria.
DR HOGENOM; CLU_125878_1_0_6; -.
DR InParanoid; P41443; -.
DR OMA; YVMFNAF; -.
DR BioCyc; EcoCyc:G7707-MON; -.
DR BioCyc; MetaCyc:G7707-MON; -.
DR PRO; PR:P41443; -.
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; IPR012902; N_methyl_site.
DR InterPro; IPR045584; Pilin-like.
DR InterPro; IPR022346; T2SS_GspH.
DR InterPro; IPR002416; T2SS_protein-GspH.
DR Pfam; PF12019; GspH; 1.
DR Pfam; PF07963; N_methyl; 1.
DR PRINTS; PR00885; BCTERIALGSPH.
DR SUPFAM; SSF54523; SSF54523; 1.
DR TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1.
DR TIGRFAMs; TIGR01708; typeII_sec_gspH; 1.
DR PROSITE; PS00409; PROKAR_NTER_METHYL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane; Methylation;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT PROPEP 1..6
FT /note="Leader sequence"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT /id="PRO_0000024216"
FT CHAIN 7..169
FT /note="Type II secretion system protein H"
FT /id="PRO_0000024217"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 7
FT /note="N-methylphenylalanine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT HELIX 34..61
FT /evidence="ECO:0007829|PDB:2KNQ"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:2KNQ"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:2KNQ"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:2KNQ"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:2KNQ"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:2KNQ"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:2KNQ"
FT STRAND 105..114
FT /evidence="ECO:0007829|PDB:2KNQ"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:2KNQ"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:2KNQ"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:2KNQ"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:2KNQ"
FT STRAND 147..158
FT /evidence="ECO:0007829|PDB:2KNQ"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:2KNQ"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:2KNQ"
SQ SEQUENCE 169 AA; 18565 MW; D42B1127FBB81A09 CRC64;
MNQQRGFTLL EMMLVLALVA ITASVVLFTY GREDVASTRA RETAARFTAA LELAIDRATL
SGQPVGIHFS DSAWRIMVPG KTPSAWRWVP LQEDAADESQ NDWDEELSIH LQPFKPDDSN
QPQVVILADG QITPFSLLMA NAGTGEPLLT LVCSGSWPLD QTLARDTRP
