ID   GSPH_KLEOK              Reviewed;         183 AA.
AC   A0A0H3H546;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Type II secretion system protein H;
DE            Short=T2SS minor pseudopilin H;
DE   AltName: Full=General secretion pathway protein H;
DE   Flags: Precursor;
GN   Name=pulH; OrderedLocusNames=KOX_13585;
OS   Klebsiella oxytoca (strain ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 /
OS   NRRL B-199 / KCTC 1686 / BUCSAV 143 / CCM 1901).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=1006551;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 / KCTC
RC   1686 / BUCSAV 143 / CCM 1901;
RA   Shin S.H., Kim S., Kim J.Y., Yang K.-S., Seo J.-S.;
RT   "Complete genome sequence of Klebsiella oxytoca strain KCTC 1686.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 / KCTC
RC   1686 / BUCSAV 143 / CCM 1901;
RX   PubMed=22493189; DOI=10.1128/jb.00026-12;
RA   Shin S.H., Kim S., Kim J.Y., Lee S., Um Y., Oh M.K., Kim Y.R., Lee J.,
RA   Yang K.S.;
RT   "Complete genome sequence of Klebsiella oxytoca KCTC 1686, used in
RT   production of 2,3-butanediol.";
RL   J. Bacteriol. 194:2371-2372(2012).
RN   [3]
RP   FUNCTION, MUTAGENESIS OF GLU-10, AND INTERACTION WITH PULM.
RX   PubMed=27260845; DOI=10.1111/mmi.13432;
RA   Nivaskumar M., Santos-Moreno J., Malosse C., Nadeau N., Chamot-Rooke J.,
RA   Tran Van Nhieu G., Francetic O.;
RT   "Pseudopilin residue E5 is essential for recruitment by the type 2
RT   secretion system assembly platform.";
RL   Mol. Microbiol. 101:924-941(2016).
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 (PubMed:27260845). Part of the
CC       pseudopilus tip complex that is critical for the recognition and
CC       binding of secretion substrates (By similarity).
CC       {ECO:0000250|UniProtKB:Q00515, ECO:0000269|PubMed:27260845}.
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 (By similarity). Interacts with PulM
CC       (PubMed:27260845). {ECO:0000250|UniProtKB:Q00515,
CC       ECO:0000269|PubMed:27260845}.
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}.
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DR   EMBL; CP003218; AEX04441.1; -; Genomic_DNA.
DR   RefSeq; WP_014228299.1; NC_016612.1.
DR   AlphaFoldDB; A0A0H3H546; -.
DR   SMR; A0A0H3H546; -.
DR   EnsemblBacteria; AEX04441; AEX04441; KOX_13585.
DR   KEGG; kox:KOX_13585; -.
DR   HOGENOM; CLU_125878_0_0_6; -.
DR   OMA; YVMFNAF; -.
DR   Proteomes; UP000007843; 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; 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   PRINTS; PR00885; BCTERIALGSPH.
DR   SUPFAM; SSF54523; SSF54523; 1.
DR   TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1.
DR   TIGRFAMs; TIGR01708; typeII_sec_gspH; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Membrane; Methylation; Transmembrane;
KW   Transmembrane helix.
FT   PROPEP          1..5
FT                   /note="Leader sequence"
FT                   /evidence="ECO:0000250|UniProtKB:Q00515"
FT                   /id="PRO_0000449528"
FT   CHAIN           6..183
FT                   /note="Type II secretion system protein H"
FT                   /id="PRO_0000449529"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         6
FT                   /note="N-methylphenylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00515"
FT   MUTAGEN         10
FT                   /note="E->A: More than 90% loss of type II secretion due to
FT                   loss of interaction with PulM."
FT                   /evidence="ECO:0000269|PubMed:27260845"
SQ   SEQUENCE   183 AA;  20341 MW;  64A74BE004F18E71 CRC64;
     MRQRGFTVLE MMLVVLLMGS AASLVIMSFP AMQQDTAERQ LQRFQAQLEF AMDSGMQNDR
     LLGIQIRPNG WQFQVLQSQA AETRSSVAHS DRWQGYVWQI WQPRQAALGG QVPDNQPLTL
     RLPPPQEWPP TAEPAADPDI LLLPGGEITP FTLIFGEKDD RSEVWLRVDE SGAIATSAKG
     GAP