ID A0A1I4G0I5_9ACTN Unreviewed; 452 AA.
AC A0A1I4G0I5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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=SAMN04488085_10877 {ECO:0000313|EMBL:SFL23229.1};
OS Geodermatophilus ruber.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=504800 {ECO:0000313|EMBL:SFL23229.1, ECO:0000313|Proteomes:UP000199152};
RN [1] {ECO:0000313|EMBL:SFL23229.1, ECO:0000313|Proteomes:UP000199152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45317 {ECO:0000313|EMBL:SFL23229.1,
RC ECO:0000313|Proteomes:UP000199152};
RA de Groot N.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; FOSW01000008; SFL23229.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4G0I5; -.
DR STRING; 504800.SAMN04488085_10877; -.
DR InParanoid; A0A1I4G0I5; -.
DR OrthoDB; 5241527at2; -.
DR Proteomes; UP000199152; 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:SFL23229.1};
KW Cilium {ECO:0000313|EMBL:SFL23229.1};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Flagellum {ECO:0000313|EMBL:SFL23229.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199152};
KW Secreted {ECO:0000256|RuleBase:RU362066}.
FT DOMAIN 11..106
FT /note="Flagellar hook-associated protein 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02465"
FT DOMAIN 204..437
FT /note="Flagellar hook-associated protein 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07195"
SQ SEQUENCE 452 AA; 45858 MW; 9D2C58F58B020EBD CRC64;
MTMSISTGLV SGMDTGALVS QLMQVEAAPQ AALKAKLTAT QTAAGAFRTV NTALQALMTA
AETALKPETW ASAKGTSSAG SVTAATAPGA TPGSLTFTVA SVAATHSTVS TTRWGSTTTA
ANLSSIEVKS LDGTTSKGTI ALNGTESLDQ VAAKINGSSN LGLKAAVVQT GTDEFALQIS
AAVSGKAGTF SLAGTETFKA TTVGQNAELK VGTTAAAYSV TSSTNVFQGV LAGTTITVTR
EETTPVTVSV VSDPDAITAK VSALVDAVNS ALDTIKKQTN NTPGSTAALR GEYAVTQISG
QLLEALSKAV GEDSPARIGF ELTRDGKLAF TKDTFTAALK DNPALAQKLM VGTPEGKDAD
GNILAAVPGI AERLRGVAKA TSDATTGTLN SLAKGQDSMA RDIQDRIAAW DVRLAKRKAA
LTRQFTAMET ALSSLQNQST WLAGQLKSLP SS
//
