ID A0A0M2UBI5_9FIRM Unreviewed; 521 AA.
AC A0A0M2UBI5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SY88_04155 {ECO:0000313|EMBL:KKM12349.1};
OS Clostridiales bacterium PH28_bin88.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=1605376 {ECO:0000313|EMBL:KKM12349.1, ECO:0000313|Proteomes:UP000034222};
RN [1] {ECO:0000313|EMBL:KKM12349.1, ECO:0000313|Proteomes:UP000034222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Robbins S., Tyson G.;
RT "High quality genome sequence of Candidatus Suratobacter aromatica.";
RL Submitted (MAR-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKM12349.1}.
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DR EMBL; LAKY01000016; KKM12349.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2UBI5; -.
DR STRING; 1605376.SY88_04155; -.
DR PATRIC; fig|1605376.3.peg.5158; -.
DR Proteomes; UP000034222; 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 Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Reference proteome {ECO:0000313|Proteomes:UP000034222};
KW Secreted {ECO:0000256|RuleBase:RU362066}.
FT DOMAIN 13..107
FT /note="Flagellar hook-associated protein 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02465"
FT DOMAIN 238..505
FT /note="Flagellar hook-associated protein 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07195"
SQ SEQUENCE 521 AA; 57490 MW; 2F739082033C0C33 CRC64;
MPYNTLRIGG LASGLDIDQI IGDMMKAERV PLDKVRQDRQ IWAWKQEDYR SMNTTLAGLR
DQVFNMKLQS TYQARKASSS NEAAVTATAG ASAADGIYTI TVRQLAEGVS KTSIATLADE
KNADNSTKTL WQQFQSHWEA QSLTSTDNIT VTINGTTLTF DLDVDNVYTA ASKINQAKLG
VTASYDAGQD RFFLTTTTTG SAATINIGSD TKLFMSDGAG DGTGALKMAL QTGTAVNGKN
AEFNLNDVVE PNRLTTSSNT FTLNGVTYTL KQGGGATSTI TVTRDGDTVY NSIKSFVDKY
NETIEKLNAE LNEERYQDYP PLTDEQRKEM KDSEIELWEE KARSGMLRND FMLRDILGNL
RTAVSTPVDD LSSEYNSLAV IGITTGSYTE GGKLYINEDK LRKAIAEYPD GVKDLFTQTD
GSDTEASSHK GVAIRLYDEL ARGIKRLSDY AGSTSGFSQV DQSFIGKELK RYDDRIQQIE
ERLQQKEDRY WKKFTALELV VSQMNTQSAW LTQQFGGGQG K
//