AAAP_ANAMF
ID AAAP_ANAMF Reviewed; 324 AA.
AC Q5SF95; B9KJ36;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Appendage-associated protein;
DE Flags: Precursor;
GN Name=aaaP1; OrderedLocusNames=AMF_659;
GN and
GN Name=aaaP2; OrderedLocusNames=AMF_663;
OS Anaplasma marginale (strain Florida).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma.
OX NCBI_TaxID=320483;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAS83465.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, 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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Florida;
RX PubMed=19134224; DOI=10.1186/1471-2164-10-16;
RA Dark M.J., Herndon D.R., Kappmeyer L.S., Gonzales M.P., Nordeen E.,
RA Palmer G.H., Knowles D.P. Jr., Brayton K.A.;
RT "Conservation in the face of diversity: multistrain analysis of an
RT intracellular bacterium.";
RL BMC Genomics 10:16-16(2009).
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; AY514451; AAS83465.1; -; Genomic_DNA.
DR EMBL; CP001079; ACM49498.1; -; Genomic_DNA.
DR EMBL; CP001079; ACM49501.1; -; Genomic_DNA.
DR RefSeq; WP_012659037.1; NC_012026.1.
DR AlphaFoldDB; Q5SF95; -.
DR STRING; 320483.AMF_659; -.
DR EnsemblBacteria; ACM49498; ACM49498; AMF_659.
DR EnsemblBacteria; ACM49501; ACM49501; AMF_663.
DR GeneID; 7397847; -.
DR KEGG; amf:AMF_659; -.
DR KEGG; amf:AMF_663; -.
DR PATRIC; fig|320483.3.peg.758; -.
DR HOGENOM; CLU_856975_0_0_5; -.
DR OrthoDB; 2126489at2; -.
DR Proteomes; UP000007307; Chromosome.
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 3: Inferred from homology;
KW Coiled coil; Reference proteome; Secreted; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000250|UniProtKB:Q5SF96"
FT CHAIN 33..324
FT /note="Appendage-associated protein"
FT /evidence="ECO:0000250|UniProtKB:Q5SF96"
FT /id="PRO_0000258015"
FT COILED 195..255
FT /evidence="ECO:0000255"
SQ SEQUENCE 324 AA; 34908 MW; 48D24D13ECF20068 CRC64;
MGCPVSRGGS PGCGRRIAEE LRLAEDARLR LALLGRCIVK GSPAQVRKEL RAELKAIDAE
WRPVIARESL RKELDAIDAE WQHAITFWHI SRAIIGSIEL SKELDAIDAE WRPVIVRESL
RKELKAIDAE WRPAIRLESA YRAIIGSIEL SKELKAIDAE TQHAVELRRA LRTIEGRIEL
SRELKAIDAE WAPRIAQAKE IAQARESLRK ELNDIDAEWA PKIAQAKEIA QAKAELAAAT
DALKRAADKL QALGKMGTTS TPGTDLIGVV TTAVTTTLAG TQPAPGTDLV GVATPSTALG
QPAPSTALTS VAAEVATPST ALGV