ID A0A2W1YKB5_9MICO Unreviewed; 484 AA.
AC A0A2W1YKB5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=DEI94_01065 {ECO:0000313|EMBL:PZF51641.1};
OS Curtobacterium sp. MCBD17_040.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=2175674 {ECO:0000313|EMBL:PZF51641.1};
RN [1] {ECO:0000313|EMBL:PZF51641.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCBD17_040 {ECO:0000313|EMBL:PZF51641.1};
RA Chase A.B., Gomez-Lunar Z., Lopez A.E., Li J., Allison S.D., Martiny A.C.,
RA Martiny J.B.H.;
RT "Emergence of Soil Bacterial Ecotypes Along a Climate Gradient.";
RL Submitted (JUN-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PZF51641.1}.
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DR EMBL; QKTL01000001; PZF51641.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W1YKB5; -.
DR OrthoDB; 5241527at2; -.
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 Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Secreted {ECO:0000256|RuleBase:RU362066}.
FT DOMAIN 37..131
FT /note="Flagellar hook-associated protein 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02465"
FT DOMAIN 241..467
FT /note="Flagellar hook-associated protein 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07195"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 484 AA; 49362 MW; 8D8DE462E7DD0019 CRC64;
MSTSGEENPM TTVSATSTPS ISVGSDGKVT ATNLVQNLDT TSIINALMTA AGVQQVQLEA
RMKTEQTNLT NYQSLNTALQ SLQTSVTGDL SANAMNLLTA TSSYSSIKAT ATTNATATQL
SLQVTQVAAK QVSVTASTGA FTGTAFTVVG ADGTQTEVNA ASTNPTDVAT AINAAKVGIA
ATAVATGTDA NGKTTYRLQL TSAQSGSSAS FSFYEGTPSD VTAGTATNLL TATGAATISS
AQDAEVTLWP GTAAAQTVTS STNVFSDIEP GLSVTVSAPT TATATITTSR DDSSISTMAG
NVVSGVNQLL SYISTQQAGT TTTAADGTTT FTAGSFTGDS MTSELYTQLQ QAIAQPVNGR
SPSAYGIAIN SDGTLSFDSS KFTTALDSDP EGTTAAIQII FGRVNTAVTA ASDPYKGYIT
NSISSQQSSI KADQATDTNW TTRLAAQKTM LTAKYTALAT TLSQMQSESS YLTQQVDQWS
SNNN
//
