ID A0A1M5R3I3_9FIRM Unreviewed; 535 AA.
AC A0A1M5R3I3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=SAMN02744040_01227 {ECO:0000313|EMBL:SHH20892.1};
OS Tepidibacter thalassicus DSM 15285.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Tepidibacter.
OX NCBI_TaxID=1123350 {ECO:0000313|EMBL:SHH20892.1, ECO:0000313|Proteomes:UP000242520};
RN [1] {ECO:0000313|Proteomes:UP000242520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15285 {ECO:0000313|Proteomes:UP000242520};
RA Varghese N., Submissions S.;
RL Submitted (NOV-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; FQXH01000010; SHH20892.1; -; Genomic_DNA.
DR RefSeq; WP_072724663.1; NZ_FQXH01000010.1.
DR AlphaFoldDB; A0A1M5R3I3; -.
DR STRING; 1123350.SAMN02744040_01227; -.
DR OrthoDB; 9776025at2; -.
DR Proteomes; UP000242520; 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; IPR010810; Flagellin_hook_IN_motif.
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; PF07196; Flagellin_IN; 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:SHH20892.1};
KW Cilium {ECO:0000313|EMBL:SHH20892.1};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Flagellum {ECO:0000313|EMBL:SHH20892.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000242520};
KW Secreted {ECO:0000256|RuleBase:RU362066}.
FT DOMAIN 12..114
FT /note="Flagellar hook-associated protein 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02465"
FT DOMAIN 222..522
FT /note="Flagellar hook-associated protein 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07195"
SQ SEQUENCE 535 AA; 59723 MW; AD9B2B9E465BD890 CRC64;
MSNIMRISGM ATGMDTESMI KQLMDAEKIR LNKYNQQKQI KKWTQEAYNN INKDIANFIL
DTKKELGVGF GGSISSASWM KKATSSDTNV FDATATSSAV SGTHSIEVRQ IASNVNKASL
SEIDDPNVDL SGKVVKFKTS SGTEITIDGF SNINELVNKI NEHSDELKIK ASYDSNFKRF
FLSTTEGGEE NIIQISEDNG NIFTGASSIL KTDLTLNEQY KGTNGEVVFD GAVITTTKNQ
FTINGINIDL KSADAGTVHT IKVDTDVDGV YDKIKGFIDK YNELIDKLNK KISEKRYRDY
QPLTDEQKKA MDEDTVKLWE EKAKSGLLRN DEHITRILSN TRSGLYEPVY SDYDAGDSGK
LSGFSFLTEI GITTGTYQEK GKLKIDETKL KDAIREDVDG VINLLFNTSD VTESEAKSDP
DKAKERRAET GLINRLYDDL ISGMKSIIDK SGTGDNASLY RQVKSTILID FVTKSGSISL
LDKDVINIEK QISRENDRLN RVENRYWRQF TALEKAMSKM NSQSSWLMSQ MGMGM
//
