ID   RICKA_RICCN             Reviewed;         517 AA.
AC   Q92H62;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Arp2/3 complex-activating protein rickA;
DE   AltName: Full=Actin polymerization protein rickA;
GN   Name=rickA; OrderedLocusNames=RC0909;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
RN   [2]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=14749835; DOI=10.1038/nature02318;
RA   Gouin E., Egile C., Dehoux P., Villiers V., Adams J., Gertler F., Li R.,
RA   Cossart P.;
RT   "The RickA protein of Rickettsia conorii activates the Arp2/3 complex.";
RL   Nature 427:457-461(2004).
CC   -!- FUNCTION: Recruits and activates the Arp2/3 complex, which in turn
CC       leads to actin polymerization, promoting Rickettsia motility during
CC       infection. {ECO:0000269|PubMed:14749835}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14749835}.
CC   -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:14749835}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL03447.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE006914; AAL03447.1; ALT_INIT; Genomic_DNA.
DR   PIR; E97813; E97813.
DR   RefSeq; WP_041471735.1; NC_003103.1.
DR   AlphaFoldDB; Q92H62; -.
DR   SMR; Q92H62; -.
DR   EnsemblBacteria; AAL03447; AAL03447; RC0909.
DR   KEGG; rco:RC0909; -.
DR   PATRIC; fig|272944.4.peg.1033; -.
DR   HOGENOM; CLU_567284_0_0_5; -.
DR   OMA; RSLPWFK; -.
DR   Proteomes; UP000000816; Chromosome.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Actin-binding.
FT   CHAIN           1..517
FT                   /note="Arp2/3 complex-activating protein rickA"
FT                   /id="PRO_0000259652"
FT   DOMAIN          406..423
FT                   /note="WH2"
FT   REGION          313..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          444..477
FT                   /note="Central and acidic domains"
FT   REGION          461..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..381
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..406
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..428
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        461..483
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..501
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..517
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   517 AA;  58359 MW;  97ED615E0957D130 CRC64;
     MVKEIDINKL LAQENNALNT ILSQVNELCK QNKQLQGLIE IQNETKELEK EHNRSLPWFK
     RFVKTVSNVK YILIKSEEQL TNEAIKYNNK ILKDIDNKIY NIAEKSAPLK QALQEEIEKN
     FKDLTKKDLS KDQRARLSEV FFSYKSKPER FSALHMTNPL QFINAEALEK QYNSLNATKQ
     NIQNLISANS NIKELKEIQK QVAEIRAEVP HTFFEKLNNI WQNVKNVFVN NSEQVLAKNK
     ESNTRTIRKI DEQLYKTKHK FEELIENKER NIKDIIAKLP DNEKLQKIVS NLTNHMASQK
     EPILANASLA KPLENNITPP SPLPENNIPS PPPPPPPSPL PENNIPSSPP PPPPPPLPEN
     NIPSPPPPPP PPPPPPMAPA QAETLSKPIE STTVKKLANQ PRPSIDTSDL MREIAGPKKL
     KKVEFDPNTG KPVAHSHSKP AQNVNALSGL ESIFARRAVI KVSDSSSSES DSGNWSDVSV
     NRNKSKMLKT KGERDAKMTT HAQKINNRNS QNPSFVR