ID A0A1H7SP70_9BURK Unreviewed; 483 AA.
AC A0A1H7SP70;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Flagellar hook-associated protein 2 {ECO:0000256|RuleBase:RU362066};
DE Short=HAP2 {ECO:0000256|RuleBase:RU362066};
DE AltName: Full=Flagellar cap protein {ECO:0000256|RuleBase:RU362066};
GN ORFNames=SAMN05192542_112148 {ECO:0000313|EMBL:SEL74268.1};
OS Paraburkholderia caballeronis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=416943 {ECO:0000313|EMBL:SEL74268.1, ECO:0000313|Proteomes:UP000199120};
RN [1] {ECO:0000313|Proteomes:UP000199120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 26416 {ECO:0000313|Proteomes:UP000199120};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for 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. {ECO:0000256|RuleBase:RU362066}.
CC -!- SUBUNIT: Homopentamer. {ECO:0000256|ARBA:ARBA00011255,
CC ECO:0000256|RuleBase:RU362066}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU362066}.
CC Bacterial flagellum {ECO:0000256|RuleBase:RU362066}.
CC -!- SIMILARITY: Belongs to the FliD family. {ECO:0000256|ARBA:ARBA00009764,
CC ECO:0000256|RuleBase:RU362066}.
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DR EMBL; FOAJ01000012; SEL74268.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7SP70; -.
DR STRING; 416943.SAMN05445871_0333; -.
DR OrthoDB; 9034667at2; -.
DR Proteomes; UP000199120; Unassembled WGS sequence.
DR GO; GO:0009421; C:bacterial-type flagellum filament cap; IEA:InterPro.
DR GO; GO:0009424; C:bacterial-type flagellum hook; IEA:UniProtKB-UniRule.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; FLAGELLAR CAP/ASSEMBLY PROTEIN FLID; 1.
DR PANTHER; PTHR30288:SF0; FLAGELLAR HOOK-ASSOCIATED PROTEIN 2; 1.
DR Pfam; PF07196; Flagellin_IN; 1.
DR Pfam; PF07195; FliD_C; 1.
DR Pfam; PF02465; FliD_N; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum {ECO:0000256|ARBA:ARBA00023143,
KW ECO:0000256|RuleBase:RU362066};
KW Cell projection {ECO:0000313|EMBL:SEL74268.1};
KW Cilium {ECO:0000313|EMBL:SEL74268.1};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Flagellum {ECO:0000313|EMBL:SEL74268.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199120};
KW Secreted {ECO:0000256|RuleBase:RU362066}.
FT DOMAIN 34..129
FT /note="Flagellar hook-associated protein 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02465"
FT DOMAIN 235..461
FT /note="Flagellar hook-associated protein 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07195"
SQ SEQUENCE 483 AA; 48490 MW; ADF7CB93FDF9AA11 CRC64;
MTSTVTTTSG TTAADLNSQL AQAAQSIIDG ATGSTLDINS LVQAMVTSKT SAQASAIATQ
QSSDNTELSA IGKIQSALSS LDDALSGFLD GTALSQVKAS LNGTGITAST TTGAVTGSYS
VSVSQLATAS SAQSIALPST STLNAGTMTL QVGSSSMNVS VTSGESLSAI ATAINNSAGN
PGVSATVVNA TDGQHLLLTS KQTGQANTIT LTSNVTATDS SGNSTALFSQ GVVAGQDAQL
SINGLQVTSA SNTVTNALTG VTLDISGVNG ATPSTPVTQT LTLVNDTSAS TTAINNFVSA
YNNYVTTAAS LSSYNQSTST AGPLLGDSMT NGITNGLASL ISSGITSGGK TYSLSSIGLN
LQPDGTISVD DDTLQNALST NSSALTAVFN PLNGIGAKLD LFMTPYTQAS GMIDQRTSTL
NADLSDLQDQ STQLTDYQNA LTAQYNAQFT ALNNLMTQMQ NNTQYLTQLF GGKDSAGTLA
SNK
//