FLA_CAMJ8
ID FLA_CAMJ8 Reviewed; 576 AA.
AC P22251; A8FN18;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Flagellin A;
GN Name=flaA; OrderedLocusNames=C8J_1256;
OS Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC
OS 11828).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=407148;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2211662; DOI=10.1016/s0021-9258(18)38234-6;
RA Nuijten P.J., van Asten F.J., Gaastra W., van der Zeijst B.A.M.;
RT "Structural and functional analysis of two Campylobacter jejuni flagellin
RT genes.";
RL J. Biol. Chem. 265:17798-17804(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81116 / NCTC 11828;
RX PubMed=17873037; DOI=10.1128/jb.01404-07;
RA Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M.,
RA van Vliet A.H.M.;
RT "The complete genome sequence of Campylobacter jejuni strain 81116
RT (NCTC11828).";
RL J. Bacteriol. 189:8402-8403(2007).
RN [3]
RP INTERACTION WITH FLIW, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=81116 / NCTC 11828;
RX PubMed=27353476; DOI=10.1111/mmi.13455;
RA Radomska K.A., Ordonez S.R., Woesten M.M., Wagenaar J.A., van Putten J.P.;
RT "Feedback control of Campylobacter jejuni flagellin levels through
RT reciprocal binding of FliW to flagellin and the global regulator CsrA.";
RL Mol. Microbiol. 102:207-220(2016).
RN [4]
RP INTERACTION WITH FLIS, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, AND
RP MUTAGENESIS OF 567-SER--GLN-576.
RC STRAIN=81116 / NCTC 11828;
RX PubMed=28659885; DOI=10.3389/fmicb.2017.01060;
RA Radomska K.A., Woesten M.M.S.M., Ordonez S.R., Wagenaar J.A.,
RA van Putten J.P.M.;
RT "Importance of Campylobacter jejuni FliS and FliW in flagella biogenesis
RT and flagellin secretion.";
RL Front. Microbiol. 8:1060-1060(2017).
CC -!- FUNCTION: Flagellin is the subunit protein which polymerizes to form
CC the filaments of bacterial flagella.
CC -!- SUBUNIT: Heteromer of FlaA and FlaB (Probable). Interacts with FliW
CC (PubMed:27353476). Interacts with FliS (PubMed:27353476).
CC {ECO:0000269|PubMed:27353476, ECO:0000269|PubMed:28659885,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27353476,
CC ECO:0000269|PubMed:28659885}. Bacterial flagellum.
CC -!- INDUCTION: Translation is inhibited by translational regulator CsrA (at
CC protein level) (PubMed:27353476). {ECO:0000269|PubMed:27353476}.
CC -!- DOMAIN: Interacts with FliS via its C-terminal domain (residues 537-
CC 576), interacts with FliW via its N-terminal domain (residues 1-44).
CC May form a 3-way complex of flagellin, FliS and FliW simultaneously, in
CC which FliS and FliW do not directly interact (By similarity).
CC {ECO:0000250|UniProtKB:P02968, ECO:0000269|PubMed:28659885}.
CC -!- DISRUPTION PHENOTYPE: In a double flaA-flaB deletion, cells grow faster
CC and are non-motile, flagellar filaments are non-existent
CC (PubMed:27353476). {ECO:0000269|PubMed:27353476}.
CC -!- SIMILARITY: Belongs to the bacterial flagellin family. {ECO:0000305}.
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DR EMBL; J05635; AAA23024.1; -; Genomic_DNA.
DR EMBL; CP000814; ABV52855.1; -; Genomic_DNA.
DR PIR; A39228; A39228.
DR RefSeq; WP_012006752.1; NC_009839.1.
DR PDB; 6X80; EM; 3.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=1-576.
DR PDBsum; 6X80; -.
DR AlphaFoldDB; P22251; -.
DR SMR; P22251; -.
DR KEGG; cju:C8J_1256; -.
DR HOGENOM; CLU_011142_7_1_7; -.
DR OMA; MAERNAM; -.
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 1: Evidence at protein level;
KW 3D-structure; Bacterial flagellum; Secreted.
FT CHAIN 1..576
FT /note="Flagellin A"
FT /id="PRO_0000182594"
FT REGION 1..44
FT /note="Required for interaction with FliW"
FT /evidence="ECO:0000269|PubMed:28659885"
FT REGION 537..576
FT /note="Required for interaction with FliS"
FT /evidence="ECO:0000269|PubMed:28659885"
FT MUTAGEN 567..576
FT /note="Missing: No longer binds FliS, binds FliW."
FT /evidence="ECO:0000269|PubMed:28659885"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:6X80"
FT HELIX 9..34
FT /evidence="ECO:0007829|PDB:6X80"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:6X80"
FT HELIX 45..99
FT /evidence="ECO:0007829|PDB:6X80"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:6X80"
FT HELIX 106..129
FT /evidence="ECO:0007829|PDB:6X80"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:6X80"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:6X80"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:6X80"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:6X80"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:6X80"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:6X80"
FT STRAND 186..197
FT /evidence="ECO:0007829|PDB:6X80"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:6X80"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:6X80"
FT HELIX 214..223
FT /evidence="ECO:0007829|PDB:6X80"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:6X80"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:6X80"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:6X80"
FT HELIX 273..279
FT /evidence="ECO:0007829|PDB:6X80"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:6X80"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:6X80"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:6X80"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:6X80"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:6X80"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:6X80"
FT STRAND 329..338
FT /evidence="ECO:0007829|PDB:6X80"
FT TURN 348..351
FT /evidence="ECO:0007829|PDB:6X80"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:6X80"
FT HELIX 365..369
FT /evidence="ECO:0007829|PDB:6X80"
FT HELIX 374..380
FT /evidence="ECO:0007829|PDB:6X80"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:6X80"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:6X80"
FT HELIX 400..405
FT /evidence="ECO:0007829|PDB:6X80"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:6X80"
FT STRAND 412..416
FT /evidence="ECO:0007829|PDB:6X80"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:6X80"
FT HELIX 425..430
FT /evidence="ECO:0007829|PDB:6X80"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:6X80"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:6X80"
FT HELIX 461..463
FT /evidence="ECO:0007829|PDB:6X80"
FT TURN 468..470
FT /evidence="ECO:0007829|PDB:6X80"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:6X80"
FT HELIX 483..536
FT /evidence="ECO:0007829|PDB:6X80"
FT HELIX 540..566
FT /evidence="ECO:0007829|PDB:6X80"
FT HELIX 567..571
FT /evidence="ECO:0007829|PDB:6X80"
FT HELIX 572..575
FT /evidence="ECO:0007829|PDB:6X80"
SQ SEQUENCE 576 AA; 59529 MW; A5E1E68BC0CBFDDB CRC64;
MGFRINTNVA ALNAKANSDL NAKSLDASLS RLSSGLRINS AADDASGMAI ADSLRSQANT
LGQAISNGND ALGILQTADK AMDEQLKILD TIKTKATQAA QDGQSLKTRT MLQADINKLM
EELDNIANTT SFNGKQLLSG NFTNQEFQIG ASSNQTVKAT IGATQSSKIG VTRFETGAQS
FTSGVVGLTI KNYNGIEDFK FDNVVISTSV GTGLGALAEE INKSADKTGV RATYDVKTTG
VYAIKEGTTS QDFAINGVTI GKIEYKDGDG NGSLISAINA VKDTTGVQAS KDENGKLVLT
SADGRGIKIT GDIGVGSGIL ANQKENYGRL SLVKNDGRDI NISGTNLSAI GMGTTDMISQ
SSVSLRESKG QISATNADAM GFNSYKGGGK FVFTQNVSSI SAFMSAQGSG FSRGSGFSVG
SGKNLSVGLS QGIQIISSAA SMSNTYVVSA GSGFSSGSGN SQFAALKTTA ANTTDETAGV
TTLKGAMAVM DIAETAITNL DQIRADIGSI QNQVTSTINN ITVTQVNVKA AESQIRDVDF
ASESANYSKA NILAQSGSYA MAQANSSQQN VLRLLQ
