FLAB_CAMCO
ID FLAB_CAMCO Reviewed; 573 AA.
AC P18245;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Flagellin B;
DE AltName: Full=Flagellin N;
GN Name=flaB;
OS Campylobacter coli.
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=195;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=VC167 T2;
RX PubMed=1856171; DOI=10.1128/jb.173.15.4757-4764.1991;
RA Guerry P., Alm R.A., Power M.E., Logan S.M., Trust T.J.;
RT "Role of two flagellin genes in Campylobacter motility.";
RL J. Bacteriol. 173:4757-4764(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2318805; DOI=10.1128/jb.172.4.1853-1860.1990;
RA Guerry P., Logan S.M., Thornton S., Trust T.J.;
RT "Genomic organization and expression of Campylobacter flagellin genes.";
RL J. Bacteriol. 172:1853-1860(1990).
CC -!- FUNCTION: Flagellin is the subunit protein which polymerizes to form
CC the filaments of bacterial flagella.
CC -!- SUBUNIT: Heteromer of FlaA and FlaB. A flagellar filament composed
CC exclusively of FlaA is indistinguishable in length from that of the
CC wild-type and shows a slight reduction in motility. The flagellar
CC filament composed exclusively of the FlaB is severely truncated in
CC length and greatly reduced in motility. Thus, while both flagellins are
CC not necessary for motility, both are required for a fully active
CC flagellar filament.
CC -!- SUBCELLULAR LOCATION: Secreted. Bacterial flagellum.
CC -!- SIMILARITY: Belongs to the bacterial flagellin family. {ECO:0000305}.
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DR EMBL; M64670; AAA23023.1; -; Genomic_DNA.
DR EMBL; M64671; AAA23027.1; -; Genomic_DNA.
DR EMBL; M35141; AAA23020.1; -; Genomic_DNA.
DR PIR; A35146; A35146.
DR PIR; B42474; B42474.
DR AlphaFoldDB; P18245; -.
DR SMR; P18245; -.
DR STRING; 1367491.BN865_08010; -.
DR eggNOG; COG1344; Bacteria.
DR GO; GO:0009288; C:bacterial-type flagellum; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR Gene3D; 6.10.10.10; -; 1.
DR InterPro; IPR001492; Flagellin.
DR InterPro; IPR046358; Flagellin_C.
DR InterPro; IPR042187; Flagellin_C_sub2.
DR InterPro; IPR010810; Flagellin_hook_IN_motif.
DR InterPro; IPR001029; Flagellin_N.
DR PANTHER; PTHR42792; PTHR42792; 1.
DR Pfam; PF00700; Flagellin_C; 1.
DR Pfam; PF07196; Flagellin_IN; 2.
DR Pfam; PF00669; Flagellin_N; 1.
DR PRINTS; PR00207; FLAGELLIN.
PE 3: Inferred from homology;
KW Bacterial flagellum; Secreted.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..573
FT /note="Flagellin B"
FT /id="PRO_0000182592"
FT VARIANT 287..288
FT /note="VQ -> IE"
FT VARIANT 302
FT /note="A -> R"
FT CONFLICT 337
FT /note="D -> N (in Ref. 2; AAA23020)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="R -> A (in Ref. 2; AAA23020)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="L -> S (in Ref. 2; AAA23020)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 573 AA; 59192 MW; EF15D6D3F65CDC43 CRC64;
MGFRINTNIG ALNAHANSVV NARELDKSLS RLSSGLRINS AADDASGMAI ADSLRSQAAT
LGQAINNGND AIGILQTADK AMDEQLKILD TIKTKATQAA QDGQSLKTRT MLQADINRLM
EELDNIANTT SFNGKQLLSG GFTNQEFQIG SSSNQTIKAS IGATQSSKIG VTRFETGSQS
FSSGTVGLTI KNYNGIEDFK FDSVVISTSV GTGLGALAEE INRNADKTGI RATFDVKSVG
AYAIKAGNTS QDFAINGVVI GQINYNDGDN NGQLISAINA VKDTTGVQAS KDENGKLVLT
SADGRGIKIT GSIGVGAGIL HTENYGRLSL VKNDGRDINI SGTGLSAIGM GATDMISQSS
VSLRESKGQI SAANADAMGF NAYNGGGAKQ IIFASSIAGF MSQAGSGFSA GSGFSVGSGK
NYSAILSASI QIVSSARSIS STYVVSTGSG FSAGSGNSQF AALRISTVSA HDETAGVTTL
KGAMAVMDIA ETAITNLDQI RADIGAVQNQ LQVTINNITV TQVNVKAAES TIRDVDFAAE
SANFSKYNIL AQSGSYAMSQ RNAVQQNVLK LLQ