ID   RICKA_RICRI             Reviewed;         494 AA.
AC   Q9AKJ0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Arp2/3 complex-activating protein rickA;
DE   AltName: Full=Actin polymerization protein rickA;
GN   Name=rickA; ORFNames=ORFB4;
OS   Rickettsia rickettsii.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=783;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=84-21C;
RX   PubMed=11319266; DOI=10.1093/oxfordjournals.molbev.a003864;
RA   Andersson J.O., Andersson S.G.E.;
RT   "Pseudogenes, junk DNA, and the dynamics of Rickettsia genomes.";
RL   Mol. Biol. Evol. 18:829-839(2001).
RN   [2]
RP   FUNCTION.
RC   STRAIN=HLP, and Norgaard;
RX   PubMed=15236643; DOI=10.1111/j.1462-5822.2004.00402.x;
RA   Jeng R.L., Goley E.D., D'Alessio J.A., Chaga O.Y., Svitkina T.M.,
RA   Borisy G.G., Heinzen R.A., Welch M.D.;
RT   "A Rickettsia WASP-like protein activates the Arp2/3 complex and mediates
RT   actin-based motility.";
RL   Cell. Microbiol. 6:761-769(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:15236643}.
CC   -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250}.
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DR   EMBL; AJ293314; CAC33668.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9AKJ0; -.
DR   SMR; Q9AKJ0; -.
DR   PRIDE; Q9AKJ0; -.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Actin-binding.
FT   CHAIN           1..494
FT                   /note="Arp2/3 complex-activating protein rickA"
FT                   /id="PRO_0000259653"
FT   DOMAIN          383..400
FT                   /note="WH2"
FT   REGION          312..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..454
FT                   /note="Central and acidic domains"
FT   COMPBIAS        314..359
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..405
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..426
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..460
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        461..478
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..494
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   494 AA;  56190 MW;  4334E4E8307A063D CRC64;
     MVKEIDINKL LAQENNALNA ILSHVNELCK QNKQLQGLIE IQNETKELEK EHNRSLPWFK
     RFVKTVSNVK YILIKSEEQL TNEAIKYNNK ILKDIDNKIY NIAEKSAPLK QALQEEIEKS
     FKDLTKKDLS KDQRARLSEV FFSYKSKPER FSALHMTNPL QFINAEALEK QFNSLNATKQ
     NIQNLISENS NIKELKEIQK QVAEIRAEVP HTFFEKLNNI WQNVKNVFVN NSEQVLAKNK
     ESNTRTIRKI DEQLYKTQHK FEELIENKER NIKDIIAKLP DNEELQKIVS NLTNHMASKK
     EPILANVSLA KPLENNIPPP PPPPPPLPDN NIPPPPPPPP PLPDNNIPPP PPPPPMAPVK
     TLSKAVEATT VKKLENQPRP SIDTSDLMRE IAGPKKLKKV EFDPNTGKPV AHSHSKPAQN
     VNKPSGLESI FARRVAIEMS DSSSSESDSG NWSDVSVNRN KSKMLKTKGE RDAKMTTHAQ
     KINNRNSQKP SFVR