ID A0A1W6N2I3_9PROT Unreviewed; 611 AA.
AC A0A1W6N2I3;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=GQ61_00150 {ECO:0000313|EMBL:ARN84025.1};
OS Candidatus Nucleicultrix amoebiphila FS5.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Holosporales;
OC Caedimonadaceae; Nucleicultrix.
OX NCBI_TaxID=1414854 {ECO:0000313|EMBL:ARN84025.1, ECO:0000313|Proteomes:UP000237351};
RN [1] {ECO:0000313|EMBL:ARN84025.1, ECO:0000313|Proteomes:UP000237351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FS5 {ECO:0000313|EMBL:ARN84025.1,
RC ECO:0000313|Proteomes:UP000237351};
RA Schulz F., Horn M.;
RT "The genome of the endonuclear symbiont Nucleicultrix amoebiphila.";
RL Submitted (JUN-2014) 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; CP008743; ARN84025.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6N2I3; -.
DR STRING; 1414854.GQ61_00150; -.
DR KEGG; naf:GQ61_00150; -.
DR OrthoDB; 9810816at2; -.
DR Proteomes; UP000237351; 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:UP000237351};
KW Secreted {ECO:0000256|RuleBase:RU362066}.
FT DOMAIN 32..137
FT /note="Flagellar hook-associated protein 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02465"
FT DOMAIN 252..590
FT /note="Flagellar hook-associated protein 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07195"
SQ SEQUENCE 611 AA; 64984 MW; E462E2E9B30230DF CRC64;
MSLQLGIGSP LTFNGADVDE NGRISLQSTV MGLDVKKTVD DVKAALEKQL DTPKKTIETI
DSKLKALSTL QTKVTTLRDA LDNLRGPAEG LTSAGIFNKL GYLVPNATYS GAVTLSLDDT
ASPQNFNLNI TQLATQDVVI AGGQIADITT DMGLTGNLTF QTTTYDSNGL PVYGTLQVTL
DGQSAQQIAD TIKMNQSLTG ITATLTQAVS GNYQFAFKEL NYGTPLTFTK NVTGGTANLV
PDSSVATADS LSAKYTVDGI AAKASSNTFN IFPGVNITLN QVTNATFQVQ LMPDVVSIKQ
AIVDFTNAYN DVYDEIKKQS ALNEAGDKKA DDAFLFGNRI LNSLKNVLAP TLASSLDGAK
NTSIITLADI GITMGSATVV TDASTGVQSK VYDGRLVIDN GILNNALNTN VTGVQKLFGF
TYQTTDSTFS VTQHPESLPT ELANNTWHVS LAKDNSGTLS AVFWYDNDPS SIQYAATIET
FSTKTAIVSG PVGSVFANIE VMIQNIDQIS NNSSRQTSIN STQGQPNKLK FALDGLLDPT
SGVGDFATQQ SLFTDQKTQQ ETKITQIQKQ IDLKRDALLQ SMQEMQMAVN AALTMQNTLT
SLLYPGAASA A
//
