ID   GSPH_KLEPN              Reviewed;         170 AA.
AC   P15747;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 2.
DT   25-MAY-2022, entry version 83.
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=Pullulanase secretion protein PulH;
DE   Flags: Precursor;
GN   Name=pulH;
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: 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 PulG. {ECO:0000250|UniProtKB:Q00515}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:Q00515}; Single-pass membrane protein
CC       {ECO:0000255}.
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   -!- SIMILARITY: Belongs to the GSP H family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA25130.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; M32613; AAA25130.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; P15747; -.
DR   SMR; P15747; -.
DR   TCDB; 3.A.15.1.1; the outer membrane protein secreting main terminal branch (mtb) family.
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; IPR012902; N_methyl_site.
DR   InterPro; IPR045584; Pilin-like.
DR   InterPro; IPR002416; T2SS_protein-GspH.
DR   Pfam; PF07963; N_methyl; 1.
DR   PRINTS; PR00885; BCTERIALGSPH.
DR   SUPFAM; SSF54523; SSF54523; 1.
DR   TIGRFAMs; TIGR01708; typeII_sec_gspH; 1.
DR   PROSITE; PS00409; PROKAR_NTER_METHYL; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Methylation;
KW   Protein transport; Transmembrane; Transmembrane helix; Transport.
FT   PROPEP          1..5
FT                   /note="Leader sequence"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT                   /id="PRO_0000024222"
FT   CHAIN           6..170
FT                   /note="Type II secretion system protein H"
FT                   /id="PRO_0000024223"
FT   TRANSMEM        6..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         6
FT                   /note="N-methylphenylalanine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
SQ   SEQUENCE   170 AA;  18403 MW;  0200CC4DF0636280 CRC64;
     MRQRGFTLLE MMLILLLMGV SAGMVLLAFP ASRDDSAAQT LARFEAQLRF VQQRGLQTGQ
     FFGVSVHPDR WQFLVLEARD GADPAPADDG WSGYRWLPLR AGRVATSGSI AGGKLNLAFA
     QGEAWTPGDN PDVLIFPGGE MTPFRLTLGE APGIAFNARG ESLPEPQEAQ