ID   GSPH_PECCC              Reviewed;         188 AA.
AC   P31587;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=Pectic enzymes secretion protein OutH;
DE   Flags: Precursor;
GN   Name=outH;
OS   Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp.
OS   carotovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SCRI 193;
RX   PubMed=8326859; DOI=10.1111/j.1365-2958.1993.tb01589.x;
RA   Reeves P.J., Whitcombe D., Wharam S., Gibson M., Allison G., Bunce N.,
RA   Barallon R., Douglas P., Mulholland V., Stevens S., Walker S.,
RA   Salmond G.P.C.;
RT   "Molecular cloning and characterization of 13 out genes from Erwinia
RT   carotovora subspecies carotovora: genes encoding members of a general
RT   secretion pathway (GSP) widespread in Gram-negative bacteria.";
RL   Mol. Microbiol. 8:443-456(1993).
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 OutG. {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}.
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DR   EMBL; X70049; CAA49649.1; -; Genomic_DNA.
DR   PIR; S32862; S32862.
DR   AlphaFoldDB; P31587; -.
DR   SMR; P31587; -.
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; TIGR02532; IV_pilin_GFxxxE; 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..10
FT                   /note="Leader sequence"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT                   /id="PRO_0000024218"
FT   CHAIN           11..188
FT                   /note="Type II secretion system protein H"
FT                   /id="PRO_0000024219"
FT   TRANSMEM        13..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         11
FT                   /note="N-methylphenylalanine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
SQ   SEQUENCE   188 AA;  21391 MW;  733E90BFDDD6C5F9 CRC64;
     MKRSTRKQQG FTLLEMMLVV LLAGIAAGMV VMAFPPERQN DSAWQLARFQ AQLEFAAESS
     QVNEYMLGVR IYPDRWQFYQ LQRPAASERI PIPSGDRWQG YKWQPWQPHR VSASATLPEA
     LRLELLQADG KKVDKTQSGD DPDILILPGG EITPFRLLVK SENKALSNWL QVDNTGRFVT
     SMSQGKKR