ID A0A1H0YM46_9BURK Unreviewed; 524 AA.
AC A0A1H0YM46;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=SAMN05443245_0163 {ECO:0000313|EMBL:SDQ16239.1};
OS Paraburkholderia fungorum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=134537 {ECO:0000313|EMBL:SDQ16239.1, ECO:0000313|Proteomes:UP000183487};
RN [1] {ECO:0000313|Proteomes:UP000183487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAS106B {ECO:0000313|Proteomes:UP000183487};
RA Varghese N.;
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; FNKP01000001; SDQ16239.1; -; Genomic_DNA.
DR RefSeq; WP_074762503.1; NZ_FNKP01000001.1.
DR AlphaFoldDB; A0A1H0YM46; -.
DR OrthoDB; 9034667at2; -.
DR Proteomes; UP000183487; 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; 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; 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:SDQ16239.1};
KW Cilium {ECO:0000313|EMBL:SDQ16239.1};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Flagellum {ECO:0000313|EMBL:SDQ16239.1};
KW Secreted {ECO:0000256|RuleBase:RU362066}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..524
FT /note="Flagellar hook-associated protein 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010318029"
FT DOMAIN 40..136
FT /note="Flagellar hook-associated protein 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02465"
FT DOMAIN 277..499
FT /note="Flagellar hook-associated protein 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07195"
SQ SEQUENCE 524 AA; 51080 MW; 25B395163000930F CRC64;
MSTISTSAST SSAAAAAAQA AAAAALQQAS QSIISGSTGS SLDVSSLVTA LVNSKIAGQT
ATLTAKATTD NTQLSAIGQL SASLSSLQVG LAPLFNGSLQ TAFTATASGT GLTATAASGA
VAGTYSVKTT QIAQGQSITS GAFTSAQTAS MGTGTLNIMV GSSSMTLAVN STNNTLSGIA
AAINNSSTNP GVAATVVNGA DGAHLVLSST TTGAANTINV NVTGASTGAA LSSLSVQSVT
GNDSDTSTFA SAADGTTTSI GASTLATGST WTQSSAAQDA VFSLNGTIAT SSTNAVTSAL
DGVTMNLASA SAGTTQTLTV AADTATQVTD IENFVSQYNA VVSTMTSLTS FDSSAAAGSQ
GGPLLGDSML DAIQNGLGNI VSSGIKGAAA GTTLASLGIT LNSDGTMSVD TTALTAAVQY
NPNQVAAVFN TSTGIAAQLN TTISAYTTTG GIIDVRTDAI TTDLDSIKDQ SNTLTAYQAQ
LTSQYNNEFT ALNTLMATTT SNSNYLTQLF GGTNSSGSMS DNKA
//
