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Alanine and proline-rich secreted protein Apa (45/47 kDa antigen) (FAP-B) (Fibronectin attachment protein)

 APA_MYCBP               Reviewed;         325 AA.
P80069; A1KJS2;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 2.
07-JUN-2017, entry version 72.
RecName: Full=Alanine and proline-rich secreted protein Apa;
AltName: Full=45/47 kDa antigen {ECO:0000303|PubMed:8423100};
AltName: Full=FAP-B;
AltName: Full=Fibronectin attachment protein;
Flags: Precursor;
Name=apa; Synonyms=modD; OrderedLocusNames=BCG_1896;
Mycobacterium bovis (strain BCG / Pasteur 1173P2).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=410289;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=BCG / Pasteur 1173P2;
PubMed=17372194; DOI=10.1073/pnas.0700869104;
Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W.,
Valenti P., Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C.,
Inwald J.K., Golby P., Garcia J.N., Hewinson R.G., Behr M.A.,
Quail M.A., Churcher C., Barrell B.G., Parkhill J., Cole S.T.;
"Genome plasticity of BCG and impact on vaccine efficacy.";
Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
[2]
PROTEIN SEQUENCE OF 40-56.
STRAIN=BCG;
PubMed=8423100;
Romain F., Laqueyrerie A., Militzer P., Pescher P., Chavarot P.,
Lagranderie M., Auregan G., Gheorghiu M., Marchal G.A.;
"Identification of a Mycobacterium bovis BCG 45/47-kilodalton antigen
complex, an immunodominant target for antibody response after
immunization with living bacteria.";
Infect. Immun. 61:742-750(1993).
[3]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH HOST
PSP-A, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
STRAIN=BCG / Pasteur 1173P2;
PubMed=17158455; DOI=10.1074/jbc.M610183200;
Ragas A., Roussel L., Puzo G., Riviere M.;
"The Mycobacterium tuberculosis cell-surface glycoprotein Apa as a
potential adhesin to colonize target cells via the innate immune
system pulmonary C-type lectin surfactant protein A.";
J. Biol. Chem. 282:5133-5142(2007).
-!- FUNCTION: Might function as an adhesin for host (human) cells.
Cell surface Apa binds to human PSP-A (SFTPA1) via its
glycosylated sites where it might down-regulate the immune
response; PSP-A probably binds other bacterial proteins as well
(PubMed:17158455). {ECO:0000269|PubMed:17158455}.
-!- SUBUNIT: Binds to human PSP-A (SFTPA1) via its glycosylated
moiety; binding disappears after treatment with alpha-mannosidase
(PubMed:17158455). {ECO:0000269|PubMed:17158455}.
-!- SUBCELLULAR LOCATION: Secreted. Cell surface
{ECO:0000269|PubMed:17158455}.
-!- PTM: Glycosylated (PubMed:17158455).
{ECO:0000269|PubMed:17158455}.
-!- PTM: Runs as 45 and 47 kDa protein, the nature of the difference
between the 2 forms is not known (PubMed:8423100,
PubMed:17158455). {ECO:0000269|PubMed:17158455,
ECO:0000269|PubMed:8423100}.
-!- SIMILARITY: Belongs to the Apa family. {ECO:0000305}.
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EMBL; AM408590; CAL71883.1; -; Genomic_DNA.
PIR; A49237; A49237.
RefSeq; WP_003409337.1; NC_008769.1.
SMR; P80069; -.
EnsemblBacteria; CAL71883; CAL71883; BCG_1896.
KEGG; mbb:BCG_1896; -.
HOGENOM; HOG000049611; -.
OMA; GEFFMPY; -.
Proteomes; UP000001472; Chromosome.
GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0050840; F:extracellular matrix binding; IEA:InterPro.
InterPro; IPR010801; FAP.
Pfam; PF07174; FAP; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Glycoprotein; Repeat;
Secreted; Signal.
SIGNAL 1 39 {ECO:0000269|PubMed:8423100}.
CHAIN 40 325 Alanine and proline-rich secreted protein
Apa.
/FTId=PRO_0000064406.
REPEAT 85 88 1.
REPEAT 94 97 2.
REPEAT 104 107 3.
REGION 85 107 3 X 4 AA approximate repeats of [DA]-P-N-
A.
CARBOHYD 49 49 O-linked (Man...) threonine.
{ECO:0000250|UniProtKB:P9WIR7}.
CARBOHYD 57 57 O-linked (Man...) threonine.
{ECO:0000250|UniProtKB:P9WIR7}.
CARBOHYD 66 66 O-linked (Man) threonine.
{ECO:0000250|UniProtKB:P9WIR7}.
CARBOHYD 316 316 O-linked (Man...) threonine.
{ECO:0000250|UniProtKB:P9WIR7}.
CONFLICT 40 40 D -> A (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 49 50 TT -> PA (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 53 53 S -> A (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 56 56 S -> A (in Ref. 2; AA sequence).
{ECO:0000305}.
SEQUENCE 325 AA; 32687 MW; D3419CA5547D91E9 CRC64;
MHQVDPNLTR RKGRLAALAI AAMASASLVT VAVPATANAD PEPAPPVPTT AASPPSTAAA
PPAPATPVAP PPPAAANTPN AQPGDPNAAP PPADPNAPPP PVIAPNAPQP VRIDNPVGGF
SFALPAGWVE SDAAHLDYGS ALLSKTTGDP PFPGQPPPVA NDTRIVLGRL DQKLYASAEA
TDSKAAARLG SDMGEFYMPY PGTRINQETV SLDANGVSGS ASYYEVKFSD PSKPNGQIWT
GVIGSPAANA PDAGPPQRWF VVWLGTANNP VDKGAAKALA ESIRPLVAPP PAPAPAPAEP
APAPAPAGEV APTPTTPTPQ RTLPA


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