ID   GSPH_DICCH              Reviewed;         181 AA.
AC   P24687;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 2.
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   Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=EC16;
RX   PubMed=1429461; DOI=10.1128/jb.174.22.7385-7397.1992;
RA   Lindeberg M., Collmer A.;
RT   "Analysis of eight out genes in a cluster required for pectic enzyme
RT   secretion by Erwinia chrysanthemi: sequence comparison with secretion genes
RT   from other Gram-negative bacteria.";
RL   J. Bacteriol. 174:7385-7397(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-181.
RC   STRAIN=EC16;
RX   PubMed=1992458; DOI=10.1073/pnas.88.3.1079;
RA   He S.Y., Lindeberg M., Chatterjee A.K., Collmer A.;
RT   "Cloned Erwinia chrysanthemi out genes enable Escherichia coli to
RT   selectively secrete a diverse family of heterologous proteins to its
RT   milieu.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:1079-1083(1991).
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; L02214; AAA24835.1; -; Genomic_DNA.
DR   EMBL; M37886; AAA24826.1; -; Genomic_DNA.
DR   PIR; F47021; F47021.
DR   AlphaFoldDB; P24687; -.
DR   SMR; P24687; -.
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..5
FT                   /note="Leader sequence"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT                   /id="PRO_0000024220"
FT   CHAIN           6..181
FT                   /note="Type II secretion system protein H"
FT                   /id="PRO_0000024221"
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   181 AA;  20288 MW;  7E72A931042B63B8 CRC64;
     MRQRGFTLLE IMLVVLLAGV AATLVMMAIP APKQQDSGWQ IARFKAQLQY AVEDSQMNDH
     ILGIYIQPHR WQYALLQRQV VENSPEEQQR LRYVWIPWQP YRMSVPSELP DSFHIELSTQ
     VGAAGDGTGF SPGNGDPHVL ILPGGEVTPF RLTLRNGNDS AWLQVDTNGQ VHTSPEAEQK
     G