ID   AAAP_ANAMM              Reviewed;         419 AA.
AC   Q5SF96; Q5PA90;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Appendage-associated protein;
DE   Flags: Precursor;
GN   Name=aaaP {ECO:0000312|EMBL:AAS83464.1}; OrderedLocusNames=AM878;
OS   Anaplasma marginale (strain St. Maries).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma.
OX   NCBI_TaxID=234826;
RN   [1] {ECO:0000312|EMBL:AAS83464.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 187-226, FUNCTION,
RP   AND SUBCELLULAR LOCATION.
RX   PubMed=15557651; DOI=10.1128/iai.72.12.7257-7264.2004;
RA   Stich R.W., Olah G.A., Brayton K.A., Brown W.C., Fecheimer M.,
RA   Green-Church K., Jittapalapong S., Kocan K.M., McGuire T.C.,
RA   Rurangirwa F.R., Palmer G.H.;
RT   "Identification of a novel Anaplasma marginale appendage-associated protein
RT   that localizes with actin filaments during intraerythrocytic infection.";
RL   Infect. Immun. 72:7257-7264(2004).
RN   [2] {ECO:0000312|EMBL:AAV86790.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=St. Maries;
RX   PubMed=15618402; DOI=10.1073/pnas.0406656102;
RA   Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L.,
RA   Palmer G.H., McGuire T.C., Knowles D.P. Jr.;
RT   "Complete genome sequencing of Anaplasma marginale reveals that the surface
RT   is skewed to two superfamilies of outer membrane proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005).
CC   -!- FUNCTION: Associates with actin filament appendages that are formed in
CC       the inclusion appendages of the parasitophorous vacuole during
CC       infection of the host erythrocyte. {ECO:0000269|PubMed:15557651}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15557651}.
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DR   EMBL; AY514450; AAS83464.1; -; Genomic_DNA.
DR   EMBL; CP000030; AAV86790.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5SF96; -.
DR   KEGG; ama:AM878; -.
DR   HOGENOM; CLU_641979_0_0_5; -.
DR   GO; GO:0020003; C:symbiont-containing vacuole; IDA:UniProtKB.
DR   GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR   GO; GO:0051701; P:biological process involved in interaction with host; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Coiled coil; Direct protein sequencing; Secreted; Signal.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..419
FT                   /note="Appendage-associated protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000258017"
FT   COILED          232..262
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   419 AA;  46142 MW;  B55C99D1049D7421 CRC64;
     MIVTYGTVGC PVSRGGSPGC GRRIAEELRL AEDARLRLAL LGRCIVKGSP AQARGELRAE
     LKAIDATIEL RKELDAIDAE WAPKIELSAE LRAIDAEWRP AIRLRSAYRA IIGRIELRKE
     LDAIDAEWAP KIELSAELKA IDAEWRPAIR LRSAYRAIIG RWELSKELKA IDAEWRPAIA
     RESLRKELDA IDAEWQHAIT FWHISRAIIG SIELSKELKA IDAKWKYVAI YERQKAQRRR
     EERAAKAREE LRKELNDIDA KWKSASAIKL RKDLRSTSEG VDHTEFALEL RATDKSGNME
     LVLKLKATDT KNQHDAIVKA IEDGFVGYAA ECGAATRELN ACGGMSTTSA PSTDLISTVV
     SAVTTGTGQQ QSAGSESQRP TECGGGGTLL SSLFALILPS SNWYCNAVLY GGFLGCLGS