ID A0A1H9L950_9GAMM Unreviewed; 468 AA.
AC A0A1H9L950;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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=SAMN03080615_03849 {ECO:0000313|EMBL:SER07976.1};
OS Amphritea atlantica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Amphritea.
OX NCBI_TaxID=355243 {ECO:0000313|EMBL:SER07976.1, ECO:0000313|Proteomes:UP000198749};
RN [1] {ECO:0000313|Proteomes:UP000198749}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18887 {ECO:0000313|Proteomes:UP000198749};
RA Varghese N., Submissions S.;
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; FOGB01000016; SER07976.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9L950; -.
DR STRING; 355243.SAMN03080615_03849; -.
DR OrthoDB; 5980200at2; -.
DR Proteomes; UP000198749; 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:SER07976.1};
KW Cilium {ECO:0000313|EMBL:SER07976.1};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Flagellum {ECO:0000313|EMBL:SER07976.1};
KW Secreted {ECO:0000256|RuleBase:RU362066}.
FT DOMAIN 10..107
FT /note="Flagellar hook-associated protein 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02465"
FT DOMAIN 224..447
FT /note="Flagellar hook-associated protein 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07195"
SQ SEQUENCE 468 AA; 49245 MW; F2B8F28B8BA69D0D CRC64;
MAISSPGIGS GIDIKSLVPD LVDASRAPTL NRLARKEATL QAELSAVGLL KSALSEFQTK
LDGLKDATTF SNRTAASSDK AIAAFSADNN AAAGSYSLEI TSLASAQKLV TQQDYVISEG
TLEFADAGGS FTVTLDGTNN ATIESVRDAI NSAEDNIGVT ATILVVNGSK RLVFNADETG
AENQLTITGT TTTGDLDIYD YNSGTATPDV NGDVATFYDQ VVAAADAVFS VDGQPMTSAT
NTITDVIPDA TITLADTNVG EPITLSISEN SSAIKNQIST LVDGYNELIA LINEQTSYNP
DSDTAGPLFG DSLIGSIERQ IRNTLTSRID NNDSSYTSLA SIGITTTSDG SLELDSGKLD
TALKDDYTGV TTLFSDDTQG VAFKIDAMLE NYLQISGTID GRTDSINAKL EGISDERTKL
DYRSAQLEAR LYKQFNAMDL LVAQLNSTGA WLSSALDNLP GVVRQTNK
//
