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Database: UniProt
Entry: F4V5J6_ECOLX
LinkDB: F4V5J6_ECOLX
Original site: F4V5J6_ECOLX 
ID   F4V5J6_ECOLX            Unreviewed;       567 AA.
AC   F4V5J6;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 35.
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};
GN   ORFNames=ECNG_00898 {ECO:0000313|EMBL:EGI39837.1};
OS   Escherichia coli TA280.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=656444 {ECO:0000313|EMBL:EGI39837.1, ECO:0000313|Proteomes:UP000004877};
RN   [1] {ECO:0000313|EMBL:EGI39837.1, ECO:0000313|Proteomes:UP000004877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TA280 {ECO:0000313|EMBL:EGI39837.1,
RC   ECO:0000313|Proteomes:UP000004877};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Escherichia coli TA280.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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; GL884370; EGI39837.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4V5J6; -.
DR   HOGENOM; CLU_022474_3_0_6; -.
DR   Proteomes; UP000004877; Unassembled WGS sequence.
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:SF5; SPI-1 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..28
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02219"
FT   CHAIN           29..567
FT                   /note="Type 3 secretion system secretin"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02219"
FT                   /id="PRO_5026396660"
FT   DOMAIN          34..102
FT                   /note="SPI-1 type 3 secretion system secretin N0"
FT                   /evidence="ECO:0000259|Pfam:PF21304"
FT   DOMAIN          180..305
FT                   /note="NolW-like"
FT                   /evidence="ECO:0000259|Pfam:PF03958"
FT   DOMAIN          362..517
FT                   /note="Type II/III secretion system secretin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00263"
SQ   SEQUENCE   567 AA;  62754 MW;  6D7924B3D97459C4 CRC64;
     MKIKLRITII LISALCIFNG LLTPGAYAAT ANGYVANKEN LRSFFETVSS YAGKPTIVSK
     LAMKKQISGN FDLTEPYALI ERLSAQMGLI WYDDGKAIYI YDSSEMRNAL INLRKVSTNE
     FNNFLKKSGL YNSRYEIKGG GNGTFYVSGP PVYVDLVVNA AKLMEQNSDG IEIGRNKVGI
     IHLVNTFVND RTYELRGEKI VIPGMAKVLS TLLNNNIKQS TGVNVLSEIS SRQQLKNVSR
     MPPFPGAEED DDLQVEKIIS TAGAPETDDI QIIAYPDTNS LLVKGTVSQV DFIEKLVATL
     DIPKRHIELS LWIIDIDKTD LEQLGADWSG TIKIGSSLSA SFNNSGSIST LDGTQFIATI
     QALAQKRRAA VVARPVVLTQ ENIPAIFDNN RTFYTKLVGE RTAELDEVTY GTMISVLPRF
     ASRNQIELLL NIEDGNEINS DKTNVDDLPQ VGRTLISTIA RVPQGKSLLI GGYTRDTNTY
     ESRKIPILGS IPFIGKLFGY EGTNANNIVR VFLIEPREID ERMMNNANEA AVDARAITQQ
     MAKNKEINDE LLQKWIKTYL NREVVGG
//
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