ID   FLIC_ECO27              Reviewed;         548 AA.
AC   B7USU2;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Flagellin;
GN   Name=fliC; OrderedLocusNames=E2348C_2041;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/jb.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA   Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA   Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-20.
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=9622352; DOI=10.1046/j.1365-2958.1998.00793.x;
RA   Farris M., Grant A., Richardson T.B., O'Connor C.D.;
RT   "BipA: a tyrosine-phosphorylated GTPase that mediates interactions between
RT   enteropathogenic Escherichia coli (EPEC) and epithelial cells.";
RL   Mol. Microbiol. 28:265-279(1998).
CC   -!- FUNCTION: Flagellin is the subunit protein which polymerizes to form
CC       the filaments of bacterial flagella. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255}. Bacterial flagellum
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the bacterial flagellin family. {ECO:0000255}.
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DR   EMBL; FM180568; CAS09589.1; -; Genomic_DNA.
DR   RefSeq; WP_000079695.1; NC_011601.1.
DR   AlphaFoldDB; B7USU2; -.
DR   SMR; B7USU2; -.
DR   EnsemblBacteria; CAS09589; CAS09589; E2348C_2041.
DR   KEGG; ecg:E2348C_2041; -.
DR   HOGENOM; CLU_011142_7_2_6; -.
DR   OMA; IASQTTY; -.
DR   Proteomes; UP000008205; Chromosome.
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; IPR001029; Flagellin_N.
DR   InterPro; IPR032826; FliC_H7.
DR   PANTHER; PTHR42792; PTHR42792; 1.
DR   Pfam; PF00700; Flagellin_C; 1.
DR   Pfam; PF00669; Flagellin_N; 1.
DR   Pfam; PF12445; FliC; 1.
DR   PRINTS; PR00207; FLAGELLIN.
PE   1: Evidence at protein level;
KW   Bacterial flagellum; Direct protein sequencing; Secreted.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9622352"
FT   CHAIN           2..548
FT                   /note="Flagellin"
FT                   /id="PRO_0000449038"
SQ   SEQUENCE   548 AA;  56301 MW;  3BFEAF63DE7B6023 CRC64;
     MAQVINTNSL SLITQNNINK NQSALSSSIE RLSSGLRINS AKDDAAGQAI ANRFTSNIKG
     LTQAARNAND GISVAQTTEG ALSEINNNLQ RIRELTVQAS TGTNSDSDLD SIQDEIKSRL
     DEIDRVSGQT QFNGVNVLAK DGSMKIQVGA NDGQTITIDL KKIDSDTLGL NGFNVNGKGE
     TANTAATLKD MSGFTAAAAP GGTVGVTQYT DKSAVASSVD ILNAVAGADG NKVTTSADVG
     FGTPAAAVTY TYNKDTNSYS AASDDISSAN LAAFLNPQAR DTTKATVTIG GKDQDVNIDK
     SGNLTAADDG AVLYMDATGN LTKNNAGGDT QATLAKVATA TGAKAATIQT DKGTFTSDGT
     AFDGASMSID ANTFANAVKN DTYTATVGAK TYSVTTGSAA ADTAYMSNGV LSDTPPTYYA
     QADGSITTTE DAAAGKLVYK GSDGKLTTDT TSKAESTSDP LAALDDAISQ IDKFRSSLGA
     VQNRLDSAVT NLNNTTTNLS EAQSRIQDAD YATEVSNMSK AQIIQQAGNS VLAKANQVPQ
     QVLSLLQG