ID A0A0U5B4H4_9BACL Unreviewed; 833 AA.
AC A0A0U5B4H4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-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=CB4_00693 {ECO:0000313|EMBL:BAU26566.1};
OS Aneurinibacillus soli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Aneurinibacillus group; Aneurinibacillus.
OX NCBI_TaxID=1500254 {ECO:0000313|EMBL:BAU26566.1, ECO:0000313|Proteomes:UP000217696};
RN [1] {ECO:0000313|EMBL:BAU26566.1, ECO:0000313|Proteomes:UP000217696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB4 {ECO:0000313|EMBL:BAU26566.1,
RC ECO:0000313|Proteomes:UP000217696};
RA Lee J.S., Lee K.C., Kim K.K., Lee B.W.;
RT "Genome sequence of Aneurinibacillus soli.";
RL Submitted (DEC-2015) 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; AP017312; BAU26566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U5B4H4; -.
DR KEGG; asoc:CB4_00693; -.
DR OrthoDB; 9776025at2; -.
DR Proteomes; UP000217696; 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 Cell projection {ECO:0000313|EMBL:BAU26566.1};
KW Cilium {ECO:0000313|EMBL:BAU26566.1};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Flagellum {ECO:0000313|EMBL:BAU26566.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000217696};
KW Secreted {ECO:0000256|RuleBase:RU362066}.
FT DOMAIN 15..110
FT /note="Flagellar hook-associated protein 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02465"
FT DOMAIN 470..819
FT /note="Flagellar hook-associated protein 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07195"
SQ SEQUENCE 833 AA; 89030 MW; 1875DEF59A1AC05E CRC64;
MASFTSLTRI SGLNSGMDTE SLVKKLMDAE SIRYNKMKQD QQKLTWQSDA YRQWNTDLFS
FRSTVSDMKF SRNYNTFSTT SSNPDAVVAT AGPDAIDGIH TIKVSQLAAS ATVKATGVKF
DVTKSLGDTS QGSPLAANDK LTISTTDGQG VSHTAQIDIK TTDKIGDVVN ALNAAKDTDG
KSLGIQAMYD SNLQQFIIKT KSTGAKTSIN ITGNDATLST FGLQNSSRYA SLQDTNATNA
TLKLNIDSTS FSADMLAIST KDSQGKVSTA QIKIEANYTV NDVLNAFNSA KDSNGNALGI
QATYDSGSKQ LTIKTNEVGA QTSLSITGTK DVSGTTLDAL GLKDASDMQS INGIDPKMTV
PVPKIVSGTP LNLADKLTIT ATDSKGMLHT AKIDIKATDT IEDIMTTLSS AKDSAGNSLG
IQATYDGASK QLVITGGNTK LGITGSNASL VALGLKDPAS PVSTISTTGV DSVITSDGST
VTQSSNSVTL FGVNYTLKQA DDTKDITVNV ARDYDAAVKN IKDFIGKYND MLDKVYKAMS
ESVDKNYQPL TDDQRQAMNQ DQIKQWEDRA KSGLLHNDTI LSTLYNKLRS DTFSTVDNGS
VYNSLAAVGI KSNGYLDRGK LTVDETKLRE ALQNDPEAVR TLFTQSKNAW KSANQVDDTA
RGLNSVKFSV GSASYTVTLD PNDTTSKVAE KINDYAKSKN ISVQASYDSG TKLFSISSSL
GQDFQFTDGA SVLGNLQDVS GGQKGIVNRM YDSFYSAFQS TIQKAGLSTS DKADQSVVGK
LLKDINKRIS DEKTRLTNVE NSYYSKFTAM EKALSQYNSQ SSALMQQLGL GGK
//