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Database: UniProt
Entry: Q93FL4_CITRO
LinkDB: Q93FL4_CITRO
Original site: Q93FL4_CITRO 
ID   Q93FL4_CITRO            Unreviewed;       512 AA.
AC   Q93FL4;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Type 3 secretion system secretin {ECO:0000256|HAMAP-Rule:MF_02219};
DE            Short=T3SS secretin {ECO:0000256|HAMAP-Rule:MF_02219};
DE   Flags: Precursor;
GN   Name=sctC {ECO:0000256|HAMAP-Rule:MF_02219};
OS   Citrobacter rodentium.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=67825 {ECO:0000313|EMBL:AAL06362.1};
RN   [1] {ECO:0000313|EMBL:AAL06362.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DBS100 {ECO:0000313|EMBL:AAL06362.1};
RX   PubMed=11553577; DOI=10.1128/IAI.69.10.6323-6335.2001;
RA   Deng W., Li Y., Vallance B.A., Finlay B.B.;
RT   "Locus of enterocyte effacement from Citrobacter rodentium: sequence
RT   analysis and evidence for horizontal transfer among attaching and effacing
RT   pathogens.";
RL   Infect. Immun. 69:6323-6335(2001).
CC   -!- FUNCTION: Component of the type III secretion system (T3SS), also
CC       called injectisome, which is used to inject bacterial effector proteins
CC       into eukaryotic host cells. Forms a ring-shaped multimeric structure
CC       with an apparent central pore in the outer membrane.
CC       {ECO:0000256|HAMAP-Rule:MF_02219}.
CC   -!- SUBUNIT: The core secretion machinery of the T3SS is composed of
CC       approximately 20 different proteins, including cytoplasmic components,
CC       a base, an export apparatus and a needle. This subunit is part of the
CC       base, which anchors the injectisome in the bacterial cell envelope.
CC       Forms a stable homooligomeric complex. {ECO:0000256|HAMAP-
CC       Rule:MF_02219}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane
CC       {ECO:0000256|ARBA:ARBA00004442, ECO:0000256|HAMAP-Rule:MF_02219,
CC       ECO:0000256|RuleBase:RU004004}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004370}.
CC   -!- SIMILARITY: Belongs to the bacterial secretin family. T3SS SctC
CC       subfamily. {ECO:0000256|ARBA:ARBA00007032, ECO:0000256|HAMAP-
CC       Rule:MF_02219}.
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DR   EMBL; AF311901; AAL06362.1; -; Genomic_DNA.
DR   RefSeq; WP_012907126.1; NZ_JXUN01000121.1.
DR   AlphaFoldDB; Q93FL4; -.
DR   SMR; Q93FL4; -.
DR   OMA; QYNGAGN; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030257; C:type III protein secretion system complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0030254; P:protein secretion by the type III secretion system; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1370.120; -; 2.
DR   Gene3D; 3.55.50.30; -; 1.
DR   HAMAP; MF_02219; Type_III_secretin; 1.
DR   InterPro; IPR005644; NolW-like.
DR   InterPro; IPR038591; NolW-like_sf.
DR   InterPro; IPR004846; T2SS/T3SS_dom.
DR   InterPro; IPR004845; T2SS_GspD_CS.
DR   InterPro; IPR049034; T3S_SPI-1_N0.
DR   InterPro; IPR003522; T3SS_OM_pore_YscC.
DR   NCBIfam; TIGR02516; type_III_yscC; 1.
DR   PANTHER; PTHR30332; PROBABLE GENERAL SECRETION PATHWAY PROTEIN D; 1.
DR   PANTHER; PTHR30332:SF4; TYPE 3 SECRETION SYSTEM SECRETIN; 1.
DR   Pfam; PF00263; Secretin; 1.
DR   Pfam; PF03958; Secretin_N; 1.
DR   Pfam; PF21304; T3S_SPI-1_N0; 1.
DR   PRINTS; PR01337; TYPE3OMGPROT.
DR   PROSITE; PS00875; T2SP_D; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane {ECO:0000256|HAMAP-Rule:MF_02219};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02219};
KW   Protein transport {ECO:0000256|HAMAP-Rule:MF_02219};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_02219};
KW   Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW   Rule:MF_02219};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_02219, ECO:0000256|RuleBase:RU004004};
KW   Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02219"
FT   CHAIN           20..512
FT                   /note="Type 3 secretion system secretin"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02219"
FT                   /id="PRO_5026399869"
FT   DOMAIN          36..101
FT                   /note="SPI-1 type 3 secretion system secretin N0"
FT                   /evidence="ECO:0000259|Pfam:PF21304"
FT   DOMAIN          180..275
FT                   /note="NolW-like"
FT                   /evidence="ECO:0000259|Pfam:PF03958"
FT   DOMAIN          336..504
FT                   /note="Type II/III secretion system secretin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00263"
SQ   SEQUENCE   512 AA;  56357 MW;  C9F3A22E4C5538D5 CRC64;
     MKKISLFIFT ALFFCNTQAA PSSLEKRLGE SEYFIITKSS PVSVILNDFA ANYSIPVFIS
     NSVNDDFSGE IKNEKPVKVL EKLSKLYHLT WYYDENILYI YKTNEISRSI ITPTYLDIDS
     LLKYLRDTIS VNKSSCNVRK ITTFNSIEVR GVPECIKYIT SLSESLDKEA QSKAKNKDVV
     KVFKLNYASA TDITYKYRDQ NVVVPGVVSI LKTMASNGSL PSTGKGAVER SGNLFDNSVN
     ISADPRLNAV VVKDREITMD IYQQLISELD IEQRQIEISV SIIDVDANDL QQLGVNWSGT
     LNAGQSSIAF NSSAAQANIS SSVISNASNF MIRVNALQQN SKAKILSQPS IITLNNMQAI
     LDKNVTFYTK VSGEKVASLE SITSGTLLRV TPRILDDTSN SLTGKRRERV RLLLDIQDGN
     QSVNQSNIQN AGSLLPEVQN SEMTTEATLS AGESLLLGGF IQDKESSSKD GIPLLSDIPV
     IGSLFSSTVK QKHSVVRLFL IKATPIRSAS SE
//
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