ID A0A126YYA5_9MICO Unreviewed; 471 AA.
AC A0A126YYA5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=AX769_05480 {ECO:0000313|EMBL:AMM19697.1};
OS Frondihabitans sp. PAMC 28766.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frondihabitans.
OX NCBI_TaxID=1795630 {ECO:0000313|EMBL:AMM19697.1, ECO:0000313|Proteomes:UP000070552};
RN [1] {ECO:0000313|EMBL:AMM19697.1, ECO:0000313|Proteomes:UP000070552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC28744 {ECO:0000313|Proteomes:UP000070552};
RA Park H.;
RT "Complete genome of Frondihabitans sp.";
RL Submitted (FEB-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; CP014513; AMM19697.1; -; Genomic_DNA.
DR RefSeq; WP_066276834.1; NZ_CP014513.1.
DR AlphaFoldDB; A0A126YYA5; -.
DR STRING; 1795630.AX769_05480; -.
DR KEGG; frp:AX769_05480; -.
DR OrthoDB; 5241527at2; -.
DR Proteomes; UP000070552; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000070552};
KW Secreted {ECO:0000256|RuleBase:RU362066}.
FT DOMAIN 14..108
FT /note="Flagellar hook-associated protein 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02465"
FT DOMAIN 226..452
FT /note="Flagellar hook-associated protein 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07195"
SQ SEQUENCE 471 AA; 46802 MW; 5CDEF071F8F92FC1 CRC64;
MASVSGLGVD GLVSGLDTTS LINSLMTAEA QPQTLLKTEV TDTQTKITAY QGLNQQIAGL
ATLATTAQSS TSLALFTTSS SDASVTSTAS ATASAGSFDL VVGAVAQAKV GVSAAMATWP
AAGASSAAAL TIVKADGTSV DITPSSNSID ALVTAVNTSS TAGVRALKVA AGTDSSGAAQ
YRIQFSSTTT GAQGDFQVYS GTSTDVAAGS ATNILTAQGS AVIKTAQDAS VTLYAGTAAE
QKITSSTNTF SDLLPGVNVT VSKASSDPVT VSVAQDATGA TAVASGLVTS LNSVFALIST
KSAVVNSTDS SGNNVVSGGP FTGDSTVRGA NDALTSAASM PINGHSPSEI GISINKDGTL
DFDSSKFATA LANDPAGTQS MLSALATRVA DASNQVSDKY SGQLTGVITG QQSLVTNLND
QVSQWDIRLA ARRTALEAQY SNLEVQLSQL NSQSSSLTSS LASVPATYTG A
//
