ID A0A0G3BMT4_9BURK Unreviewed; 627 AA.
AC A0A0G3BMT4;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=AAW51_1144 {ECO:0000313|EMBL:AKJ27835.1};
OS Caldimonas brevitalea.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Caldimonas.
OX NCBI_TaxID=413882 {ECO:0000313|EMBL:AKJ27835.1, ECO:0000313|Proteomes:UP000035352};
RN [1] {ECO:0000313|EMBL:AKJ27835.1, ECO:0000313|Proteomes:UP000035352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7029 {ECO:0000313|EMBL:AKJ27835.1,
RC ECO:0000313|Proteomes:UP000035352};
RA Tang B., Yu Y.;
RL Submitted (MAY-2015) 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 {ECO:0000256|HAMAP-
CC Rule:MF_02219, ECO:0000256|RuleBase:RU004004}.
CC -!- SIMILARITY: Belongs to the bacterial secretin family. T3SS SctC
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_02219}.
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DR EMBL; CP011371; AKJ27835.1; -; Genomic_DNA.
DR RefSeq; WP_053013361.1; NZ_CP011371.1.
DR AlphaFoldDB; A0A0G3BMT4; -.
DR STRING; 413882.AAW51_1144; -.
DR KEGG; pbh:AAW51_1144; -.
DR PATRIC; fig|413882.6.peg.1206; -.
DR OrthoDB; 9775455at2; -.
DR Proteomes; UP000035352; Chromosome.
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; 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.
PE 3: Inferred from homology;
KW Cell outer membrane {ECO:0000256|HAMAP-Rule:MF_02219};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_02219};
KW Protein transport {ECO:0000256|HAMAP-Rule:MF_02219};
KW Reference proteome {ECO:0000313|Proteomes:UP000035352};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_02219};
KW Translocation {ECO:0000256|HAMAP-Rule:MF_02219};
KW Transport {ECO:0000256|HAMAP-Rule:MF_02219, ECO:0000256|RuleBase:RU004004}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02219"
FT CHAIN 17..627
FT /note="Type 3 secretion system secretin"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02219"
FT /id="PRO_5026407978"
FT DOMAIN 34..99
FT /note="SPI-1 type 3 secretion system secretin N0"
FT /evidence="ECO:0000259|Pfam:PF21304"
FT DOMAIN 176..314
FT /note="NolW-like"
FT /evidence="ECO:0000259|Pfam:PF03958"
FT DOMAIN 387..544
FT /note="Type II/III secretion system secretin-like"
FT /evidence="ECO:0000259|Pfam:PF00263"
FT REGION 211..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 627 AA; 66744 MW; C037301AFD801E83 CRC64;
MRLLAKLIAS CLLATAALPP AFGETAFSNK RFVYRADGKK LNEVFQDFAA SQSLPLVIDD
GVAGTVNAEF NAKPEEFLNA MSRTYGVIWY FDGTTLFIYP SKAMSSRVFR MRGYDRAQVR
EMLKSLGLGD ARFPLRFNEA EQTLLAYGPP RHIELVSTVI DTLERSSRDR IGKAIQVFPL
KYAYAADRMS GSTRIPGLAS TLNNIFSGNE RSGSGLSESK GRGVAAPVAS PVDKRRSAEE
LFGIRPPDYP AASPSASANP AAKTDPSSGG SGNADPERPF FQADEATNSI IVRAMPERMK
QYETLIQQLD VAQDLVEIEA TIIDVSTDEF ESLGIEWDFT REGRGRITVS PGAPASNGQG
TSTALGGANI TTVVGDAGRA LLTRIKALEG NGKARILARP KVLGAANRMA SMVDKRVASV
RVAGNLDANL FTIEAGTSLE VLPQIVMQPD RREVRLSLFI EDGSFEGAVV DQVPIIKRTE
IRTEATIREG ESLLVGGISV ESDSKGRTGL PGLSRIPLIG AAFRHDENVK TRSERLFLLT
PKVISVAQPA KPAPVPSIEP PAGATPAPQA YGAAKPAARL ALSEPVQQPV PAPVIPVAAT
QRATADCPAA ALGLSTAACA TSARGAR
//
