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Database: UniProt
Entry: A0A1Y1R5X6_9GAMM
LinkDB: A0A1Y1R5X6_9GAMM
Original site: A0A1Y1R5X6_9GAMM 
ID   A0A1Y1R5X6_9GAMM        Unreviewed;       127 AA.
AC   A0A1Y1R5X6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=B0D91_04925 {ECO:0000313|EMBL:OQX38134.1};
OS   Oceanospirillales bacterium LUC14_002_19_P2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales.
OX   NCBI_TaxID=1940822 {ECO:0000313|EMBL:OQX38134.1, ECO:0000313|Proteomes:UP000192421};
RN   [1] {ECO:0000313|EMBL:OQX38134.1, ECO:0000313|Proteomes:UP000192421}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LUC14_002_19_P2 {ECO:0000313|EMBL:OQX38134.1};
RA   Lim S.J., Davis B.G., Gill D.E., Engel A.S., Anderson L.C., Campbell B.J.;
RT   "Novel co-symbiosis in the unique lucinid bivalve Phacoides pectinatus.";
RL   Submitted (FEB-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQX38134.1}.
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DR   EMBL; MUIA01000152; OQX38134.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1R5X6; -.
DR   Proteomes; UP000192421; Unassembled WGS sequence.
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; IPR002416; T2SS_protein-GspH.
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   PRINTS; PR00885; BCTERIALGSPH.
DR   SUPFAM; SSF54523; Pili subunits; 1.
DR   PROSITE; PS00409; PROKAR_NTER_METHYL; 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:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Methylation {ECO:0000256|RuleBase:RU368030};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192421};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          41..122
FT                   /note="Type II secretion system protein GspI C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02501"
SQ   SEQUENCE   127 AA;  14162 MW;  32936AC7F509D37A CRC64;
     MRRMSGFTLL EVMIALVIFA VAASALLLSD GNAVKRTAQI QDRVVANWLA DQAINHFYQD
     ADNLQVGSFG GPQVMSGRDW YVQSDVTETD KAGFYRVEVT VFAGNQLPEN KKEAIWDLTG
     FLHKPLR
//
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