GSPG_KLEPN
ID GSPG_KLEPN Reviewed; 140 AA.
AC P15746;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Type II secretion system core protein G;
DE Short=T2SS core protein G;
DE AltName: Full=General secretion pathway protein G;
DE AltName: Full=Pullulanase secretion protein PulG;
DE Flags: Precursor;
GN Name=pulG;
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=UNF 5023;
RX PubMed=2129543; DOI=10.1007/bf00633815;
RA Reyss I., Pugsley A.P.;
RT "Five additional genes in the pulC-O operon of the Gram-negative bacterium
RT Klebsiella oxytoca UNF5023 which are required for pullulanase secretion.";
RL Mol. Gen. Genet. 222:176-184(1990).
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 -!- 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 -!- SIMILARITY: Belongs to the GSP G family. {ECO:0000305}.
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DR EMBL; M32613; AAA25129.1; -; Genomic_DNA.
DR PDB; 1T92; X-ray; 1.60 A; A/B=31-138.
DR PDBsum; 1T92; -.
DR AlphaFoldDB; P15746; -.
DR SMR; P15746; -.
DR TCDB; 3.A.15.1.1; the outer membrane protein secreting main terminal branch (mtb) family.
DR EvolutionaryTrace; P15746; -.
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; IEA:InterPro.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IEA:InterPro.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane; Methylation;
KW Protein transport; Transmembrane; Transmembrane helix; Transport.
FT PROPEP 1..6
FT /note="Leader sequence"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT /id="PRO_0000449508"
FT CHAIN 7..140
FT /note="Type II secretion system core protein G"
FT /id="PRO_0000024207"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 120..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="N-methylphenylalanine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT HELIX 33..60
FT /evidence="ECO:0007829|PDB:1T92"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:1T92"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:1T92"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1T92"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:1T92"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:1T92"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1T92"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1T92"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:1T92"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1T92"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:1T92"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:1T92"
SQ SEQUENCE 140 AA; 15373 MW; 44264C2B5AA369B0 CRC64;
MQRQRGFTLL EIMVVIVILG VLASLVVPNL MGNKEKADRQ KVVSDLVALE GALDMYKLDN
SRYPTTEQGL QALVSAPSAE PHARNYPEGG YIRRLPQDPW GSDYQLLSPG QHGQVDIFSL
GPDGVPESND DIGNWTIGKK