ID A0A1X9YCA3_9SPHN Unreviewed; 140 AA.
AC A0A1X9YCA3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Type II secretion system protein I {ECO:0000256|RuleBase:RU368030};
DE Short=T2SS minor pseudopilin I {ECO:0000256|RuleBase:RU368030};
GN ORFNames=KC8_04075 {ECO:0000313|EMBL:ARS26468.1};
OS Sphingomonas sp. KC8.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1030157 {ECO:0000313|EMBL:ARS26468.1, ECO:0000313|Proteomes:UP000194475};
RN [1] {ECO:0000313|EMBL:ARS26468.1, ECO:0000313|Proteomes:UP000194475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KC8 {ECO:0000313|EMBL:ARS26468.1};
RA Chen Y.-L., Yu C.-P., Hu A., Lee T.-H., Yang F.-C., Ismail W., Wang P.-H.,
RA Wang C.-H., Goh K.-S., Shih C.-J., Chiang Y.-R.;
RT "Bacteria use an extradiol dioxygenase-mediated pathway to degrade natural
RT estrogens in aquatic ecosystems.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|RuleBase:RU368030}.
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.
CC {ECO:0000256|RuleBase:RU368030}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004377, ECO:0000256|RuleBase:RU368030}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004377,
CC ECO:0000256|RuleBase:RU368030}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- PTM: Cleaved by prepilin peptidase. {ECO:0000256|RuleBase:RU368030}.
CC -!- SIMILARITY: Belongs to the GSP I family.
CC {ECO:0000256|ARBA:ARBA00008358, ECO:0000256|RuleBase:RU368030}.
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DR EMBL; CP016306; ARS26468.1; -; Genomic_DNA.
DR RefSeq; WP_010127281.1; NZ_CP016306.1.
DR AlphaFoldDB; A0A1X9YCA3; -.
DR STRING; 1030157.GCA_000214335_00607; -.
DR KEGG; spkc:KC8_04075; -.
DR eggNOG; COG4967; Bacteria.
DR OrthoDB; 7189314at2; -.
DR Proteomes; UP000194475; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015627; C:type II protein secretion system complex; IEA:UniProtKB-UniRule.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1300.30; GSPII I/J protein-like; 1.
DR InterPro; IPR012902; N_methyl_site.
DR InterPro; IPR045584; Pilin-like.
DR InterPro; IPR003413; T2SS_GspI_C.
DR InterPro; IPR010052; T2SS_protein-GspI.
DR NCBIfam; TIGR01707; gspI; 1.
DR NCBIfam; TIGR02532; IV_pilin_GFxxxE; 1.
DR PANTHER; PTHR38779; TYPE II SECRETION SYSTEM PROTEIN I-RELATED; 1.
DR PANTHER; PTHR38779:SF2; TYPE II SECRETION SYSTEM PROTEIN I-RELATED; 1.
DR Pfam; PF07963; N_methyl; 1.
DR Pfam; PF02501; T2SSI; 1.
DR SUPFAM; SSF54523; Pili subunits; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519,
KW ECO:0000256|RuleBase:RU368030};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022519,
KW ECO:0000256|RuleBase:RU368030};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368030};
KW Methylation {ECO:0000256|RuleBase:RU368030};
KW Reference proteome {ECO:0000313|Proteomes:UP000194475};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU368030};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU368030}.
FT TRANSMEM 26..48
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368030"
FT DOMAIN 61..135
FT /note="Type II secretion system protein GspI C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02501"
SQ SEQUENCE 140 AA; 14942 MW; 8F1FF243E34442BE CRC64;
MSAPEHASPQ RSAEHGFGSI QRFTEYGFTL IELMVALAVF SIAALALLRL EGATLSSTAT
LSDHSIGQIV ARNLAVEVLT DPVPPTFGEI SGEANNAGRI WRWTRKADRA GELNLQTIEI
AVVDDAGQPA GALTVFRPMP
//