ID   RICKA_RICBR             Reviewed;         518 AA.
AC   Q1RI78;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Arp2/3 complex-activating protein rickA;
DE   AltName: Full=Actin polymerization protein rickA;
GN   Name=rickA; OrderedLocusNames=RBE_0855;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
CC   -!- FUNCTION: Recruits and activates the Arp2/3 complex, which in turn
CC       leads to actin polymerization, promoting Rickettsia motility during
CC       infection. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250}.
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DR   EMBL; CP000087; ABE04936.1; -; Genomic_DNA.
DR   RefSeq; WP_011477521.1; NC_007940.1.
DR   AlphaFoldDB; Q1RI78; -.
DR   STRING; 336407.RBE_0855; -.
DR   EnsemblBacteria; ABE04936; ABE04936; RBE_0855.
DR   KEGG; rbe:RBE_0855; -.
DR   eggNOG; COG1196; Bacteria.
DR   HOGENOM; CLU_567284_0_0_5; -.
DR   OMA; RSLPWFK; -.
DR   OrthoDB; 376499at2; -.
DR   Proteomes; UP000001951; Chromosome.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR003124; WH2_dom.
DR   PROSITE; PS51082; WH2; 1.
PE   3: Inferred from homology;
KW   Actin-binding.
FT   CHAIN           1..518
FT                   /note="Arp2/3 complex-activating protein rickA"
FT                   /id="PRO_0000259654"
FT   DOMAIN          424..441
FT                   /note="WH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT   REGION          310..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..338
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..359
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..404
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..433
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..461
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        478..500
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..518
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   518 AA;  58376 MW;  D3E35076A9A4BF6E CRC64;
     MAKITELDHH LNQEKEALDK VVSNLNELCE HNQKLQGFIE IQKEVKELKK EHIKSLSWFK
     KLINTVSNIK YVFVKSEEQL AKDAIEQNNK LLKRIDNTIL SVADKSGPLK QELQKELRKN
     FENLAKKDLS KDQRERLSNL LNNEYAANPQ KFAQLPMSKP LHFPNAEELE NQHNDLKVIQ
     QNVLNLLTEN SNIEELKKIQ KQVAEIREEV PFTKLEKLNN FWQKIKNIFV NNSEQVLAKN
     KENNTKTIIN IEEKLHKANN KFFELVSNKK QDIENIISNL PDSKRLEAIK EKLQKHINVK
     DTNNIAEQAS AAQLQSAETK PTAVVLPNNA IPTTPPVTEE KTFTPPPAPP PPMPTDNIPT
     PLPVSKAEAT EHKNVETAAS NVPPPPPPPM PTGNVPPPPP VGDNTVTSTP QKAKETNQPR
     PAVDTTNLMK QIQGGFNLKK IEYGEDGKPI PKNKEDTKET SDPIIAALNK IRSAKVSSDS
     ERSNSDSGTD SGWASDVSTR SKKVLTRRER NAKQSQQR