ID   GSPI_KLEOK              Reviewed;         121 AA.
AC   A0A0H3HA88;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Type II secretion system protein I;
DE            Short=T2SS minor pseudopilin I;
DE   AltName: Full=Putative general secretion pathway protein I;
DE   Flags: Precursor;
GN   Name=pulI; OrderedLocusNames=KOX_13590;
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;
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   [2]
RP   FUNCTION, INTERACTION WITH PULJ AND PULH, DISRUPTION PHENOTYPE, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=22157749; DOI=10.1038/emboj.2011.454;
RA   Cisneros D.A., Bond P.J., Pugsley A.P., Campos M., Francetic O.;
RT   "Minor pseudopilin self-assembly primes type II secretion pseudopilus
RT   elongation.";
RL   EMBO J. 31:1041-1053(2012).
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 (By similarity). Part of the pseudopilus
CC       tip complex that is critical for the recognition and binding of
CC       secretion substrates (PubMed:22493189). {ECO:0000250|UniProtKB:Q00516,
CC       ECO:0000269|PubMed:22493189}.
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 pseudopilins PulJ
CC       and PulK (PubMed:22157749). {ECO:0000250|UniProtKB:Q00516,
CC       ECO:0000269|PubMed:22157749}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:22157749}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- PTM: Cleaved by prepilin peptidase. {ECO:0000250|UniProtKB:Q00516}.
CC   -!- PTM: Methylated by prepilin peptidase at the amino group of the N-
CC       terminal methionine once the leader sequence is cleaved by prepilin
CC       peptidase. {ECO:0000250|UniProtKB:Q00516}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant shows longer pili but their
CC       number is reduced. {ECO:0000269|PubMed:22157749}.
CC   -!- SIMILARITY: Belongs to the GSP I family. {ECO:0000305}.
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DR   EMBL; CP003218; AEX04442.1; -; Genomic_DNA.
DR   RefSeq; WP_014228300.1; NC_016612.1.
DR   AlphaFoldDB; A0A0H3HA88; -.
DR   SMR; A0A0H3HA88; -.
DR   EnsemblBacteria; AEX04442; AEX04442; KOX_13590.
DR   KEGG; kox:KOX_13590; -.
DR   HOGENOM; CLU_121289_3_1_6; -.
DR   OMA; QMSAVDH; -.
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; IPR003413; T2SS_GspI_C.
DR   InterPro; IPR010052; T2SS_protein-GspI.
DR   PANTHER; PTHR38779; PTHR38779; 1.
DR   Pfam; PF07963; N_methyl; 1.
DR   Pfam; PF02501; T2SSI; 1.
DR   SUPFAM; SSF54523; SSF54523; 1.
DR   TIGRFAMs; TIGR01707; gspI; 1.
DR   TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1.
DR   PROSITE; PS00409; PROKAR_NTER_METHYL; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Membrane; Methylation; Transmembrane;
KW   Transmembrane helix.
FT   PROPEP          1..6
FT                   /note="Leader sequence"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT                   /id="PRO_0000449547"
FT   CHAIN           7..121
FT                   /note="Type II secretion system protein I"
FT                   /id="PRO_0000449548"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         7
FT                   /note="N-methylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P15748,
FT                   ECO:0000255|PROSITE-ProRule:PRU01070"
SQ   SEQUENCE   121 AA;  13721 MW;  BF5CA169F9B7E2E9 CRC64;
     MNKQKGMTLL EVLVALAIFS LAGLTLLQTT AQQARNAGMM KEKMLASWLA DNQQVRLHLN
     KLWPEKSATG ALVTYAGEEW YLSWQGVDTE FSQLRALDIE VRRHKQDTAA IFSLRSYVVH
     E