ID A0A518RIG1_9SPHN Unreviewed; 478 AA.
AC A0A518RIG1;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
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=FPZ54_15175 {ECO:0000313|EMBL:QDX27214.1};
OS Sphingomonas suaedae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=2599297 {ECO:0000313|EMBL:QDX27214.1, ECO:0000313|Proteomes:UP000318055};
RN [1] {ECO:0000313|EMBL:QDX27214.1, ECO:0000313|Proteomes:UP000318055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XS-10 {ECO:0000313|EMBL:QDX27214.1,
RC ECO:0000313|Proteomes:UP000318055};
RA Zhang H., Xu L., Zhang J.-X., Sun J.-Q.;
RT "Sphingomonas alkalisoli sp. nov., isolated from rhizosphere soil of
RT Suaedae salsa.";
RL Submitted (JUL-2019) 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; CP042239; QDX27214.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A518RIG1; -.
DR KEGG; ssua:FPZ54_15175; -.
DR OrthoDB; 7388356at2; -.
DR Proteomes; UP000318055; 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 Cell projection {ECO:0000313|EMBL:QDX27214.1};
KW Cilium {ECO:0000313|EMBL:QDX27214.1};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Flagellum {ECO:0000313|EMBL:QDX27214.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000318055};
KW Secreted {ECO:0000256|RuleBase:RU362066}.
FT DOMAIN 14..112
FT /note="Flagellar hook-associated protein 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02465"
FT DOMAIN 237..460
FT /note="Flagellar hook-associated protein 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07195"
SQ SEQUENCE 478 AA; 48218 MW; 888F8D9B71E5A7BA CRC64;
MAIESIAKTI GTGSGIDTTA LVQSLVDAQF EPKNAQITAR EEKLTAQITA ASTHKANITG
FASALTTLTR GGTLSTQPTS SNSAILGVSR LAGADLANLN AKVEVRQLAA AQSAASAPVA
DRTAAVGQGV LTLTLGTATV VDGTMTGFVP GEGDPVAIAI GPEDASLDGI AAKINAANAG
VTASILTDAD GARLVIKGAS GEERAFTLAA TETVGQEGLA ALAVGVGATG TTIGSAASDA
IVAIDGVALR RDSNSISDLV PGVRLDLAAA QPGTIISIGK SLPTSALIQA AQDFVATYNE
MLSGLNVDLD PMGGALRADS AAKTLKRQLQ QLTVAQITSG ANGTPTTLAQ IGIRTERDGS
LTVDTTALTR ALVDYPDAVE KMFAEPVGSS ATANGVAGAL NAIATEAAST VRGLGASELS
YSRSKTDLAD AKADALEAAE SLRTRMTRQF ATMDAKVAAY KSTMTFLENQ VDAWNKQD
//
