ID A0A1S6IYK0_9FIRM Unreviewed; 628 AA.
AC A0A1S6IYK0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=B0537_12535 {ECO:0000313|EMBL:AQS59836.1};
OS Desulforamulus ferrireducens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=1833852 {ECO:0000313|EMBL:AQS59836.1, ECO:0000313|Proteomes:UP000189464};
RN [1] {ECO:0000313|EMBL:AQS59836.1, ECO:0000313|Proteomes:UP000189464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSS09 {ECO:0000313|EMBL:AQS59836.1,
RC ECO:0000313|Proteomes:UP000189464};
RX PubMed=27153808; DOI=10.1099/ijsem.0.001139;
RA Yang G., Guo J., Zhuang L., Yuan Y., Zhou S.;
RT "Desulfotomaculum ferrireducens sp. nov., a moderately thermophilic
RT sulfate-reducing and dissimilatory Fe(III)-reducing bacterium isolated from
RT compost.";
RL Int. J. Syst. Evol. Microbiol. 66:3022-3028(2016).
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; CP019698; AQS59836.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S6IYK0; -.
DR STRING; 1833852.B0537_12535; -.
DR KEGG; dfg:B0537_12535; -.
DR OrthoDB; 9776025at2; -.
DR Proteomes; UP000189464; 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 Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Reference proteome {ECO:0000313|Proteomes:UP000189464};
KW Secreted {ECO:0000256|RuleBase:RU362066}.
FT DOMAIN 12..108
FT /note="Flagellar hook-associated protein 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02465"
FT DOMAIN 367..616
FT /note="Flagellar hook-associated protein 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07195"
SQ SEQUENCE 628 AA; 69719 MW; 2AEFA1095BA45073 CRC64;
MSFNMRIGGL ASGMDIDQLV SDLMKVERLK VDKLQQQRQI LEWQQEDFRT INSALRTFRD
KQVFNLRLTS TFQTRVATTS NKDAVAVSAG AGAAEGVHSI KVDRLAQGAA ITGNTIGSSS
NKSNLKSQIS GLEDQQELII NGTVFKFDAT KESIYDVVRR INNQKVEGVT SHITKTAVEP
DKENNIEGEN QVQTLDFSEN CLVAGLIIKI GDKSIGLYDG TNIESEAKLA MGVDYAYKVD
ELKEAANPTE ALVNKIISDL GADNDKYELS MSTSDGFTTL TITSKEKGIS KAVTATVTGG
KAWDVRASYD ETLDRFFLTT AKTGKDQRID VDNTTLSDAL KITAGQKLYT SDIEGSEVPE
GVIYQQGTNA KVVIDGLVID DVYTSNNFTL NGVTYSIYNT TETAVKVTIS LDTEGVYNSI
KSFVDEYNKI LELIEGKLNE KRYKDYTWPL TDEQREKLTD DQIDQWKERA RSGLLRNDDT
LRQIRDQLRL TVAALAKIGI TTTADYTTGK LEITEQGDRI LREAIANDIE GVMELFTNST
QGVAQKLSNS IGSTINTIID KAGMSGNKTD DQSFLGKRID DLNDSIDAWE VRLKQIEDRY
WQRFTAMEKA LSKMNQQSLW LMQQFGLG
//