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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
 
 
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