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FLGB_SALTY
ID   FLGB_SALTY              Reviewed;         138 AA.
AC   P16437;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Flagellar basal body rod protein FlgB;
DE   AltName: Full=Putative proximal rod protein;
GN   Name=flgB; Synonyms=fla FII, flbA; OrderedLocusNames=STM1174;
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=2129540; DOI=10.1016/0022-2836(90)90365-s;
RA   Homma M., Kutsukake K., Hasebe M., Iino T., Macnab R.M.;
RT   "FlgB, FlgC, FlgF and FlgG. A family of structurally related proteins in
RT   the flagellar basal body of Salmonella typhimurium.";
RL   J. Mol. Biol. 211:465-477(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RX   PubMed=2404955; DOI=10.1128/jb.172.2.741-747.1990;
RA   Kutsukake K., Ohya Y., Iino T.;
RT   "Transcriptional analysis of the flagellar regulon of Salmonella
RT   typhimurium.";
RL   J. Bacteriol. 172:741-747(1990).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-66.
RC   STRAIN=LT2;
RX   PubMed=8200538; DOI=10.1016/0378-1119(94)90603-3;
RA   Kutsukake K., Okada T., Yokoseki T., Iino T.;
RT   "Sequence analysis of the flgA gene and its adjacent region in Salmonella
RT   typhimurium, and identification of another flagellar gene, flgN.";
RL   Gene 143:49-54(1994).
RN   [5]
RP   PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=SJW1103;
RX   PubMed=2181149; DOI=10.1016/0022-2836(90)90132-6;
RA   Jones C.J., Macnab R.M., Okino H., Aizawa S.;
RT   "Stoichiometric analysis of the flagellar hook-(basal-body) complex of
RT   Salmonella typhimurium.";
RL   J. Mol. Biol. 212:377-387(1990).
RN   [6]
RP   ERRATUM OF PUBMED:2181149, AND SEQUENCE REVISION OF N-TERMINUS.
RA   Jones C.J., Macnab R.M., Okino H., Aizawa S.;
RL   J. Mol. Biol. 215:331-331(1990).
RN   [7]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 29595 / ST1;
RX   PubMed=2407720; DOI=10.1128/jb.172.3.1327-1339.1990;
RA   Jones C.J., Macnab R.M.;
RT   "Flagellar assembly in Salmonella typhimurium: analysis with temperature-
RT   sensitive mutants.";
RL   J. Bacteriol. 172:1327-1339(1990).
RN   [8]
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=SJW1103;
RX   PubMed=1640458; DOI=10.1016/0022-2836(92)90958-m;
RA   Kubori T., Shimamoto N., Yamaguchi S., Namba K., Aizawa S.;
RT   "Morphological pathway of flagellar assembly in Salmonella typhimurium.";
RL   J. Mol. Biol. 226:433-446(1992).
RN   [9]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 29595 / ST1;
RX   PubMed=1594581; DOI=10.1073/pnas.89.11.4801;
RA   Sosinsky G.E., Francis N.R., DeRosier D.J., Wall J.S., Simon M.N.,
RA   Hainfeld J.;
RT   "Mass determination and estimation of subunit stoichiometry of the
RT   bacterial hook-basal body flagellar complex of Salmonella typhimurium by
RT   scanning transmission electron microscopy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:4801-4805(1992).
RN   [10]
RP   FUNCTION, SUBUNIT, INTERACTION WITH FLIE, AND SUBCELLULAR LOCATION.
RC   STRAIN=SJW1103;
RX   PubMed=10809679; DOI=10.1128/jb.182.11.3029-3036.2000;
RA   Minamino T., Yamaguchi S., Macnab R.M.;
RT   "Interaction between FliE and FlgB, a proximal rod component of the
RT   flagellar basal body of Salmonella.";
RL   J. Bacteriol. 182:3029-3036(2000).
RN   [11]
RP   INTERACTION WITH FLGJ, AND SUBCELLULAR LOCATION.
RX   PubMed=11554792; DOI=10.1006/jmbi.2001.4963;
RA   Hirano T., Minamino T., Macnab R.M.;
RT   "The role in flagellar rod assembly of the N-terminal domain of Salmonella
RT   FlgJ, a flagellum-specific muramidase.";
RL   J. Mol. Biol. 312:359-369(2001).
CC   -!- FUNCTION: Structural component of flagellum, the bacterial motility
CC       apparatus. Part of the rod structure of flagellar basal body.
CC       {ECO:0000269|PubMed:10809679, ECO:0000269|PubMed:1594581,
CC       ECO:0000269|PubMed:1640458, ECO:0000269|PubMed:2181149,
CC       ECO:0000269|PubMed:2407720}.
CC   -!- SUBUNIT: The basal body constitutes a major portion of the flagellar
CC       organelle and consists of a number of rings mounted on a central rod.
CC       In Gram-negative bacteria, at least four rings, L, P, S and M are
CC       present, whereas Gram-positive bacteria lack the L and P rings. The rod
CC       consists of about 26 subunits of FlgG in the distal portion, and FlgB,
CC       FlgC and FlgF build up the proximal portion of the rod with about 6
CC       subunits each. Rod assembly occurs by export via the flagellum-specific
CC       pathway of its constituent proteins and by their incorporation into the
CC       rod structure in the probable order of FlgB, FlgC, FlgF and FlgG.
CC       Another protein, FliE, also assembles onto the stable rod structure.
CC       Interacts with FliE and peptidoglycan hydrolase FlgJ (via N-terminus),
CC       which seems to function as a scaffold or cap for rod assembly.
CC       {ECO:0000269|PubMed:10809679, ECO:0000269|PubMed:11554792,
CC       ECO:0000269|PubMed:1594581, ECO:0000269|PubMed:1640458,
CC       ECO:0000269|PubMed:2181149, ECO:0000269|PubMed:2407720}.
CC   -!- SUBCELLULAR LOCATION: Bacterial flagellum basal body
CC       {ECO:0000269|PubMed:10809679, ECO:0000269|PubMed:11554792,
CC       ECO:0000269|PubMed:1594581, ECO:0000269|PubMed:1640458,
CC       ECO:0000269|PubMed:2181149, ECO:0000269|PubMed:2407720}.
CC   -!- DISRUPTION PHENOTYPE: Defects in flagellar assembly process.
CC       {ECO:0000269|PubMed:1640458}.
CC   -!- SIMILARITY: Belongs to the flagella basal body rod proteins family.
CC       {ECO:0000305}.
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DR   EMBL; X52093; CAA36309.1; -; Genomic_DNA.
DR   EMBL; D13703; BAA02861.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL20104.1; -; Genomic_DNA.
DR   EMBL; D25292; BAA21014.1; -; Genomic_DNA.
DR   PIR; S08171; XMEBFB.
DR   RefSeq; NP_460145.1; NC_003197.2.
DR   RefSeq; WP_000887043.1; NC_003197.2.
DR   PDB; 7BIN; EM; 3.20 A; Q/R/S/T/U=1-138.
DR   PDB; 7CG0; EM; 3.20 A; k/l/m/n/o=1-138.
DR   PDB; 7CGO; EM; 3.90 A; k/l/m/n/o=1-138.
DR   PDB; 7E80; EM; 3.67 A; k/l/m/n/o=1-138.
DR   PDB; 7E82; EM; 3.30 A; k/l/m/n/o=1-138.
DR   PDBsum; 7BIN; -.
DR   PDBsum; 7CG0; -.
DR   PDBsum; 7CGO; -.
DR   PDBsum; 7E80; -.
DR   PDBsum; 7E82; -.
DR   AlphaFoldDB; P16437; -.
DR   SMR; P16437; -.
DR   STRING; 99287.STM1174; -.
DR   PaxDb; P16437; -.
DR   PRIDE; P16437; -.
DR   EnsemblBacteria; AAL20104; AAL20104; STM1174.
DR   GeneID; 1252692; -.
DR   KEGG; stm:STM1174; -.
DR   PATRIC; fig|99287.12.peg.1242; -.
DR   HOGENOM; CLU_125463_1_0_6; -.
DR   OMA; GHMARND; -.
DR   PhylomeDB; P16437; -.
DR   BioCyc; SENT99287:STM1174-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0030694; C:bacterial-type flagellum basal body, rod; IEA:InterPro.
DR   GO; GO:0071978; P:bacterial-type flagellum-dependent swarming motility; IBA:GO_Central.
DR   InterPro; IPR001444; Flag_bb_rod_N.
DR   InterPro; IPR019776; Flagellar_basal_body_rod_CS.
DR   InterPro; IPR006300; FlgB.
DR   PANTHER; PTHR30435:SF12; PTHR30435:SF12; 1.
DR   Pfam; PF00460; Flg_bb_rod; 1.
DR   PIRSF; PIRSF002889; Rod_FlgB; 1.
DR   TIGRFAMs; TIGR01396; FlgB; 1.
DR   PROSITE; PS00588; FLAGELLA_BB_ROD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Bacterial flagellum; Direct protein sequencing;
KW   Reference proteome.
FT   CHAIN           1..138
FT                   /note="Flagellar basal body rod protein FlgB"
FT                   /id="PRO_0000180792"
FT   TURN            6..8
FT                   /evidence="ECO:0007829|PDB:7BIN"
FT   HELIX           10..31
FT                   /evidence="ECO:0007829|PDB:7BIN"
FT   TURN            32..34
FT                   /evidence="ECO:0007829|PDB:7BIN"
FT   HELIX           45..55
FT                   /evidence="ECO:0007829|PDB:7BIN"
FT   STRAND          86..88
FT                   /evidence="ECO:0007829|PDB:7CG0"
FT   STRAND          95..97
FT                   /evidence="ECO:0007829|PDB:7BIN"
FT   HELIX           102..133
FT                   /evidence="ECO:0007829|PDB:7BIN"
SQ   SEQUENCE   138 AA;  15129 MW;  5964A5B727BE3770 CRC64;
     MLDRLDAALR FQQEALNLRA QRQEILAANI ANADTPGYQA RDIDFASELK KVMVRGREET
     GGVALTLTSS HHIPAQAVSS PAVDLLYRVP DQPSLDGNTV DMDRERTQFA DNSLKYQMGL
     TVLGSQLKGM MNVLQGGN
 
 
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