ID   RICKA_RICMO             Reviewed;         602 AA.
AC   Q9AKP3;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Arp2/3 complex-activating protein rickA;
DE   AltName: Full=Actin polymerization protein rickA;
GN   Name=rickA;
OS   Rickettsia montanensis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=33991;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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   EXPRESSION.
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:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250}.
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DR   EMBL; AJ293315; CAC33605.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9AKP3; -.
DR   SMR; Q9AKP3; -.
DR   PRIDE; Q9AKP3; -.
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..602
FT                   /note="Arp2/3 complex-activating protein rickA"
FT                   /id="PRO_0000259656"
FT   DOMAIN          472..489
FT                   /note="WH2 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT   DOMAIN          499..516
FT                   /note="WH2 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT   REGION          307..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          516..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          537..570
FT                   /note="Central and acidic domains"
FT   REGION          555..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..444
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..576
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   602 AA;  67490 MW;  8B9F9ABE8B159C5D CRC64;
     MTKEIDINKL LAQENNALNT ILSQVNELCE QNKQLQGLIE IQNETKALEK EYNRSLPWFK
     RFVNTVSNVK YIFIKSEEQL TNEAIKYNNK ILKDIDNKIY NIAEKSVSLK QELQEEIEKN
     FKDLTKKDLS KDQRERLSEV FFSYKSKPER FSALHMTNPL QFINAEELEK QYNSLNATKQ
     NIQNLISENS NVKELKEIQK QVAEIREEVP YTFFEKLNNI WQNVKNVFVN NSEQVLAKNK
     ESNTRTIRKI DEQLYKTKHK FEELIENKER NINDIIAKLP DNEELQKIVS NLTNHMASTK
     EPILTNSSLA KPLENNITPP PPLPGNNIPS PPPPPPPLPG NNIPSPPPPP PPLPGNNIPS
     PPPPPPPLPG NNIPSPPPPP PPLSGNNIPS PPPPPPPLSG NNIPSPPPPP PPLPGNNIPS
     PPPPPPPLSQ NNIPPPPPPP MAPVSAQTEK LSKPVEATTV KKPENQPRPS IDTSDLMREI
     AGPKKLRKVE ETDVKVQDSR DLLLQSIRGE HKLKKVEFDP NTGKPVAHSH SKPVQNVNKL
     SGVASILARR VVMEMSDSSG SESDSGNWSD VGVNRNTKTL KTKRERRKIL NNRNSQKPSF
     VK