ID A0A1G6CYX5_9FIRM Unreviewed; 831 AA.
AC A0A1G6CYX5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=SAMN02910298_01855 {ECO:0000313|EMBL:SDB38049.1};
OS Pseudobutyrivibrio sp. YE44.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Pseudobutyrivibrio.
OX NCBI_TaxID=1520802 {ECO:0000313|EMBL:SDB38049.1, ECO:0000313|Proteomes:UP000198713};
RN [1] {ECO:0000313|Proteomes:UP000198713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YE44 {ECO:0000313|Proteomes:UP000198713};
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; FMXT01000005; SDB38049.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6CYX5; -.
DR STRING; 1520802.SAMN02910298_01855; -.
DR OrthoDB; 9776025at2; -.
DR Proteomes; UP000198713; 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 Cell projection {ECO:0000313|EMBL:SDB38049.1};
KW Cilium {ECO:0000313|EMBL:SDB38049.1};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362066};
KW Flagellum {ECO:0000313|EMBL:SDB38049.1};
KW Secreted {ECO:0000256|RuleBase:RU362066}.
FT DOMAIN 10..105
FT /note="Flagellar hook-associated protein 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02465"
FT DOMAIN 557..820
FT /note="Flagellar hook-associated protein 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07195"
FT COILED 609..664
FT /evidence="ECO:0000256|RuleBase:RU362066"
SQ SEQUENCE 831 AA; 91172 MW; C6CF4379A2EB7121 CRC64;
MPIRISGLTS GLDTESIVGA LVSAYSYKKD KYVKAQTKVS WKQDAWKALN TKVYSLYTSV
GSMRYSSNYA VKKTTVSDTT KAKATASGTA INGTQSLKIN KLASTAYITG AQLEGNVTGS
STLASLGIKT DSSGEKASIS LRTGTKVTNV DIEGSMTINQ FVNKLKDAGV EANFDEKNRR
FYISAKTSGK AGDFTLSANT SMGLSSLTKL GLLSGEEISD IKDSASSAGM AKKVMPFTVD
GNSSKLMDST ELKTLLTSVM EYKKDPSSVT DADKIAEYDS IVSYLEENYG EEGVINWEDM
TEDELSELVG NVYKDAAYDT TGTKVNTATR SLIYTVGEGD DKKTYTLSGS LADIKSKLQS
LATATDEEST ALKEYLNKKY SDEVYKTTRD ENNNIVVEKY GSGGTIDWDN LDDEKLSKLA
EDVYTSGTYD ISNDATYKEL QTSINAVRDG YLAVAAAKAL PQKTSEEIAI RSEKLREAQE
QLSTALADPT NAKWAKYVEE NFGAQNSEYD SSYSDFWTQT DNIDLISSVY YRVDLAANIQ
AGNVDIDPGN VAKKVDGADA EIELNGVVYT NGTNSITVNG LTIEAMATTG DSEITVTVNN
DIDGIYDKVK DFLTQYNNLM NEMQKLYNAD SAKDYEPLTD DEKAEMSEDQ IEKWEQKIKD
SLLRRDNSLS SIISAMTMSM MKTIEIDGKT YAWSTFGVHT LGNMNAEKNE GYAYHIDGDS
EDTYTSGKTD KLRTALAEEP DVVIEFLKQM TSNLYSAMDE KMKSTSVKSV YTVYNDKEMA
SEYSSYSTLI KTWQDRVTDM EDAYYKKFAK MESALAQLQS NSSSITSMLG G
//