ADP2_MYCGA
ID ADP2_MYCGA Reviewed; 1122 AA.
AC Q9REM8;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Adhesin P1;
DE AltName: Full=Adherence protein A;
DE AltName: Full=Attachment protein;
DE AltName: Full=Cytadhesin P1;
DE Flags: Precursor;
GN Name=gapA; OrderedLocusNames=MYCGA1800; ORFNames=MGA_0934;
OS Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS (Mycoplasmoides gallisepticum).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=710127;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R(low / passage 15 / clone 2);
RX PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT "The complete genome sequence of the avian pathogen Mycoplasma
RT gallisepticum strain R(low).";
RL Microbiology 149:2307-2316(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 94-1122.
RC STRAIN=R(low);
RX PubMed=11083776; DOI=10.1128/iai.68.12.6643-6649.2000;
RA Papazisi L., Troy K.E., Gorton T.S., Liao X., Geary S.J.;
RT "Analysis of cytadherence-deficient, GapA-negative Mycoplasma gallisepticum
RT strain R.";
RL Infect. Immun. 68:6643-6649(2000).
CC -!- FUNCTION: Could be involved in cytadherence. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the adhesin P1 family. {ECO:0000305}.
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DR EMBL; AE015450; AAP56530.2; -; Genomic_DNA.
DR EMBL; AF214004; AAF25381.1; -; Genomic_DNA.
DR RefSeq; WP_011113412.1; NC_004829.2.
DR AlphaFoldDB; Q9REM8; -.
DR SMR; Q9REM8; -.
DR KEGG; mga:MGA_0934; -.
DR PATRIC; fig|233150.7.peg.197; -.
DR HOGENOM; CLU_279639_0_0_14; -.
DR OMA; VENMAFI; -.
DR OrthoDB; 1540677at2; -.
DR Proteomes; UP000001418; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020035; P:adhesion of symbiont to microvasculature; IEA:UniProtKB-KW.
DR InterPro; IPR022400; Adhesin_P1.
DR InterPro; IPR022116; P1_N.
DR Pfam; PF12378; CytadhesinP1; 1.
DR TIGRFAMs; TIGR03839; termin_org_P1; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cytadherence; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..1122
FT /note="Adhesin P1"
FT /id="PRO_0000020630"
FT TRANSMEM 1001..1021
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 182..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1113
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 337
FT /note="F -> C (in Ref. 2; AAF25381)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="T -> A (in Ref. 2; AAF25381)"
FT /evidence="ECO:0000305"
FT CONFLICT 826
FT /note="V -> A (in Ref. 2; AAF25381)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1122 AA; 121388 MW; E57D27A7FBD360AD CRC64;
MKKLIFKLSV GITPLALIGL GSFGLAVSGA KPNNLKPVNQ VGEMNSQGQS NLLEKARRWR
NSNFTSLSID GTNPGALVLT GSKSISRIDL YGNVIWTFDP GNTNDLTGKV GFYDANNRLT
AFSGDVPFNV SDLSSKTVVE ATQDQEDPNV FYLLLIPDAA VQQEQKTKDQ VFENYFMSDA
PATGDTSAEG SATPAGGGSS SSAAGGGAVA PAAASSTARL VEEGNSAGMG TMTPTASTSE
TVIDYNSDQN KIPKPKTLLD SSESSESING GRTYANINTQ NNLQGVIVKV NENLFNSENP
FAVENMAFIK PKDMVDNYPS TWTQGSANGK MTNVLQFYKH DNPNAVNNRF YRAKYYPKRL
ETQTTTPLID SSFSPYEHPE WYEDNQFVMP WMQYITNLGG LYAKDGMVYL FGGNGTWVNN
ESALSIGVFR TKFENRTAEA PGNTKTVGYP YGILLSAISF DATRNGLALA PASLGQDVGY
HFVPRLAVGG VSSPRGANGN IFLGSAITWG TNGGNFLDTK WHSPAVIEDA PTTFVTVNSS
GALQNSGNPQ PTSTPMPNSN GNESIPYRWT NSYDYNSVRF AALISKPAGG NTKQVESLFT
TALKLDTLNS LPNKFTQENN IFFSYAMLDG RQWSLGTRKD SAWLTTNTIN NFTYNTQQQL
ASTVAGENAN PRNILNALTT AKGFDRRDIG NVVYTYSNNT NKFTYYYQVG GAITTWPEVQ
VNYKTSANIT YYNLTRTDFG STTPATQDAN TVSSKLNGAY LSSTGDQQGW YNGSIYVKKA
SFTPSSQGYT WQDFKGLTTT ASNAVISNWT KAGYSIRPDD DTVFNVSKIP FEKEITAAVN
VRSLDSYYVQ LNGETSVNTV ARVSPDSSAL ALNPNRITNP LMNRDNVIGQ GAFISRNDIP
SSFFENKIND IVTTEADGKE VLDSKYINSI YRYTPPQNNP DIRLRLLVID RSRATNDFIK
LLPQVLVDGE YVAVPQANSV FVSDQEFTGF DALPGYVLPV AISIPIIIIA LALALGLGIG
IPMSQNRKML KQGFAISNKK VDILTTAVGS VFKQIINRTS VTNIKKTPQM LQANKKDGAS
SPSKPSAPAA KKPAGPTKPS APGAKPTAPA KPKAPAPTKK IE