ID A0A6I5YNW7_9SPHN Unreviewed; 471 AA.
AC A0A6I5YNW7;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 03-MAY-2023, entry version 8.
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 Name=fliD {ECO:0000313|EMBL:QGP79962.1};
GN ORFNames=GL174_13965 {ECO:0000313|EMBL:QGP79962.1};
OS Sphingobium sp. CAP-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=2676077 {ECO:0000313|EMBL:QGP79962.1, ECO:0000313|Proteomes:UP000426201};
RN [1] {ECO:0000313|EMBL:QGP79962.1, ECO:0000313|Proteomes:UP000426201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAP-1 {ECO:0000313|EMBL:QGP79962.1,
RC ECO:0000313|Proteomes:UP000426201};
RA Ma X., Liang B., Wang A.;
RT "A novel pathway for chloramphenicol metabolism in Sphingobium sp. CAP-1.";
RL Submitted (NOV-2019) 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; CP046252; QGP79962.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6I5YNW7; -.
DR Proteomes; UP000426201; Chromosome min1.
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:QGP79962.1};
KW Cilium {ECO:0000313|EMBL:QGP79962.1};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Flagellum {ECO:0000313|EMBL:QGP79962.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000426201};
KW Secreted {ECO:0000256|RuleBase:RU362066}.
FT DOMAIN 16..113
FT /note="Flagellar hook-associated protein 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02465"
FT DOMAIN 227..452
FT /note="Flagellar hook-associated protein 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07195"
SQ SEQUENCE 471 AA; 48531 MW; 0FA1F9D8989BB1D1 CRC64;
MSSIGSSILT SLGAGSGIDT ASLVSSLVSA TREPRQTAIT SNQTLNSSRI SALASAISSL
DTFADALSEV LSTSAYTGTP NSNDTSIASV SLLSGGTPTG LPAQLTVEQL ATARVLSSST
VTGATSSTAV GTGTLTITTA SGTKTITIDS TNNSYAGLAS AINASNSGVT ARVVTDSQGT
RLVFKGETGA DNDFSISTSA DDGGNVLAGL GWSGTDSSTM TSSSAPQNAK ITLDGVAYEY
ADNSIDDAIP YLRIDLNKAS PGTTVNLTMT QPTSGLADLL KEFVDAYNTL MKALNTATAA
GTDSSTSGVL NGVSGVRDMK KQLSALTSTE LSSTGTYKTL ADIGVGTNRD GTLTLDTDRL
AQALESDPEG VTNMVNPQGS GSTATGLSKL MDSVRDNIEK DDGPIKLAQE RYDKLADDYT
DQLSKLDDQM TNYEEHLTKV YAAMETRLSA LKATQSYLQQ QIDAWNNSSD N
//
