ID   RICKA_RICFE             Reviewed;         526 AA.
AC   Q4UMI6;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Arp2/3 complex-activating protein rickA;
DE   AltName: Full=Actin polymerization protein rickA;
GN   Name=rickA; OrderedLocusNames=RF_0371;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAY61222.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000053; AAY61222.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_039594871.1; NC_007109.1.
DR   AlphaFoldDB; Q4UMI6; -.
DR   STRING; 315456.RF_0371; -.
DR   PRIDE; Q4UMI6; -.
DR   EnsemblBacteria; AAY61222; AAY61222; RF_0371.
DR   KEGG; rfe:RF_0371; -.
DR   eggNOG; COG1196; Bacteria.
DR   HOGENOM; CLU_567284_0_0_5; -.
DR   OrthoDB; 376499at2; -.
DR   Proteomes; UP000008548; 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   SMART; SM00246; WH2; 2.
DR   PROSITE; PS51082; WH2; 2.
PE   3: Inferred from homology;
KW   Actin-binding; Repeat.
FT   CHAIN           1..526
FT                   /note="Arp2/3 complex-activating protein rickA"
FT                   /id="PRO_0000259655"
FT   DOMAIN          383..400
FT                   /note="WH2 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT   DOMAIN          410..427
FT                   /note="WH2 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT   REGION          305..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          425..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          448..484
FT                   /note="Central and acidic domains"
FT   REGION          464..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..354
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..493
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..526
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   526 AA;  59855 MW;  F7AA7EDED7258F4A CRC64;
     MAKEIDINKL LAQENNALNT ILSQVNELCE QNKKLQGLIE IQNETKELEK EHNRSLPWFK
     RLVKTVSNVK YIFVKSEEQL TNEAIKYNNK ILKDIDNKIY NIAEKSAPLK QELQEEIEKN
     FKDLTKKDLS KEQRERLSEV YFSYKSKPER FSALNMTNPL QFIKAEELEK QYNSLNATKQ
     NIQNLISENS NIKELKEIQK QVAEIREEIP YTFFEKLNNI WQNVKNVFVN NSEQVLAKNK
     ESNTRAIRKI DEQLYKTKHK FEELIENKER NINDIIAKLP DNEELQKIVS NLANHMTSKK
     EPILTTSSIA KPLENNVTPP PPLTKNNIPP PPPPPPLSKN NILPPPPPPM PTMAPAQTET
     LSKPVGVTTT VKKLENQPRP SIDTSDLMRE IAGPKNLRKV EKTDVKTQDS RDLLLQSIRG
     EHKLRKVEFD PNTGKPVAHS HSKPAQNVSK PNGVASILAR RVAMEMSDSS SSSGSESDSG
     NWSDASVNSN KPKALKTRGE RDAKTTTHAQ KILSNRSSQK PSFVRS