FLID_SALTY
ID FLID_SALTY Reviewed; 467 AA.
AC P16328;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Flagellar hook-associated protein 2;
DE Short=HAP2;
DE AltName: Full=Filament cap protein;
DE AltName: Full=Flagellar cap protein;
GN Name=fliD; Synonyms=flaV, flbC; OrderedLocusNames=STM1960;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2193164; DOI=10.1016/s0022-2836(05)80266-9;
RA Homma M., Derosier D.J., Macnab R.M.;
RT "Flagellar hook and hook-associated proteins of Salmonella typhimurium and
RT their relationship to other axial components of the flagellum.";
RL J. Mol. Biol. 213:819-832(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 441-467.
RC STRAIN=SJW1103;
RX PubMed=1527488; DOI=10.1099/00221287-138-6-1051;
RA Kawagishi I., Mueller V., Williams A.W., Irikura V.M., Macnab R.M.;
RT "Subdivision of flagellar region III of the Escherichia coli and Salmonella
RT typhimurium chromosomes and identification of two additional flagellar
RT genes.";
RL J. Gen. Microbiol. 138:1051-1065(1992).
RN [4]
RP SUBUNIT.
RX PubMed=9878359; DOI=10.1006/jmbi.1998.2274;
RA Vonderviszt F., Imada K., Furukawa Y., Uedaira H., Taniguchi H., Namba K.;
RT "Mechanism of self-association and filament capping by flagellar HAP2.";
RL J. Mol. Biol. 284:1399-1416(1998).
RN [5]
RP SUBUNIT.
RX PubMed=11118149; DOI=10.1126/science.290.5499.2148;
RA Yonekura K., Maki S., Morgan D.G., DeRosier D.J., Vonderviszt F., Imada K.,
RA Namba K.;
RT "The bacterial flagellar cap as the rotary promoter of flagellin self-
RT assembly.";
RL Science 290:2148-2152(2000).
CC -!- FUNCTION: Required for the morphogenesis and for the elongation of the
CC flagellar filament by facilitating polymerization of the flagellin
CC monomers at the tip of growing filament. Forms a capping structure,
CC which prevents flagellin subunits (transported through the central
CC channel of the flagellum) from leaking out without polymerization at
CC the distal end.
CC -!- SUBUNIT: Homopentamer. {ECO:0000269|PubMed:11118149,
CC ECO:0000269|PubMed:9878359}.
CC -!- INTERACTION:
CC P16328; P0A1N2: fliT; NbExp=4; IntAct=EBI-15850928, EBI-15610664;
CC -!- SUBCELLULAR LOCATION: Secreted. Bacterial flagellum.
CC -!- SIMILARITY: Belongs to the FliD family. {ECO:0000305}.
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DR EMBL; X51740; CAA36030.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20872.1; -; Genomic_DNA.
DR EMBL; M85241; AAA27076.1; -; Genomic_DNA.
DR PIR; S10364; S10364.
DR RefSeq; NP_460913.1; NC_003197.2.
DR RefSeq; WP_000146802.1; NC_003197.2.
DR PDB; 5GNA; X-ray; 2.30 A; B=401-467.
DR PDB; 5H5T; X-ray; 2.50 A; A/B/C/D/E=71-268.
DR PDB; 5KRW; NMR; -; A=428-467.
DR PDB; 6CH2; X-ray; 2.70 A; D/E/F=428-467.
DR PDBsum; 5GNA; -.
DR PDBsum; 5H5T; -.
DR PDBsum; 5KRW; -.
DR PDBsum; 6CH2; -.
DR AlphaFoldDB; P16328; -.
DR SMR; P16328; -.
DR DIP; DIP-60505N; -.
DR IntAct; P16328; 1.
DR STRING; 99287.STM1960; -.
DR PaxDb; P16328; -.
DR EnsemblBacteria; AAL20872; AAL20872; STM1960.
DR GeneID; 1253481; -.
DR KEGG; stm:STM1960; -.
DR PATRIC; fig|99287.12.peg.2076; -.
DR HOGENOM; CLU_015182_8_1_6; -.
DR OMA; GGRQQIW; -.
DR PhylomeDB; P16328; -.
DR BioCyc; SENT99287:STM1960-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0009421; C:bacterial-type flagellum filament cap; IBA:GO_Central.
DR GO; GO:0009424; C:bacterial-type flagellum hook; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR InterPro; IPR010810; Flagellin_hook_IN_motif.
DR InterPro; IPR040026; FliD.
DR InterPro; IPR010809; FliD_C.
DR InterPro; IPR003481; FliD_N.
DR PANTHER; PTHR30288; PTHR30288; 1.
DR Pfam; PF07196; Flagellin_IN; 1.
DR Pfam; PF07195; FliD_C; 1.
DR Pfam; PF02465; FliD_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial flagellum; Coiled coil; Reference proteome;
KW Secreted.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..467
FT /note="Flagellar hook-associated protein 2"
FT /id="PRO_0000177024"
FT COILED 411..439
FT /evidence="ECO:0000255"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:5H5T"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:5H5T"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:5H5T"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:5H5T"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:5H5T"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:5H5T"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:5H5T"
FT HELIX 153..162
FT /evidence="ECO:0007829|PDB:5H5T"
FT STRAND 165..175
FT /evidence="ECO:0007829|PDB:5H5T"
FT STRAND 178..188
FT /evidence="ECO:0007829|PDB:5H5T"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:5H5T"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:5H5T"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:5H5T"
FT TURN 211..214
FT /evidence="ECO:0007829|PDB:5H5T"
FT STRAND 215..222
FT /evidence="ECO:0007829|PDB:5H5T"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:5H5T"
FT STRAND 234..243
FT /evidence="ECO:0007829|PDB:5H5T"
FT TURN 246..249
FT /evidence="ECO:0007829|PDB:5H5T"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:5H5T"
FT STRAND 258..266
FT /evidence="ECO:0007829|PDB:5H5T"
FT HELIX 415..465
FT /evidence="ECO:0007829|PDB:5GNA"
SQ SEQUENCE 467 AA; 49835 MW; 5C1BD69A1F233BEA CRC64;
MASISSLGVG SNLPLDQLLT DLTKNEKGRL TPITKQQSAN SAKLTAYGTL KSALEKFQTA
NTALNKADLF KSTVASSTTE DLKVSTTAGA AAGTYKINVT QLAAAQSLAT KTTFATTKEQ
LGDTSVTSRT IKIEQPGRKE PLEIKLDKGD TSMEAIRDAI NDADSGIAAS IVKVKENEFQ
LVLTANSGTD NTMKITVEGD TKLNDLLAYD STTNTGNMQE LVKAENAKLN VNGIDIERQS
NTVTDAPQGI TLTLTKKVTD ATVTVTKDDT KAKEAIKSWV DAYNSLVDTF SSLTKYTAVE
PGEEASDKNG ALLGDSVVRT IQTGIRAQFA NSGSNSAFKT MAEIGITQDG TSGKLKIDDD
KLTKVLKDNT AAARELLVGD GKETGITTKI ATEVKSYLAD DGIIDNAQDN VNATLKSLTK
QYLSVSNSID ETVARYKAQF TQLDTMMSKL NNTSSYLTQQ FTAMNKS