ADP1_MYCPN
ID ADP1_MYCPN Reviewed; 1627 AA.
AC P11311;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Adhesin P1;
DE AltName: Full=Attachment protein;
DE AltName: Full=Cytadhesin P1;
DE Flags: Precursor;
GN Name=mgpA; OrderedLocusNames=MPN_141; ORFNames=MP013;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 29342 / M129;
RX PubMed=3119495; DOI=10.1128/iai.55.12.3023-3029.1987;
RA Su C.-J., Tryon V.V., Baseman J.B.;
RT "Cloning and sequence analysis of cytadhesin P1 gene from Mycoplasma
RT pneumoniae.";
RL Infect. Immun. 55:3023-3029(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2841195; DOI=10.1016/0378-1119(88)90337-x;
RA Inamine J.M., Denny T.P., Loechel S., Schaper U., Huang C.H., Bott K.F.,
RA Hu P.C.;
RT "Nucleotide sequence of the P1 attachment-protein gene of Mycoplasma
RT pneumoniae.";
RL Gene 64:217-229(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1301-1520.
RC STRAIN=ATCC 29342 / M129;
RX PubMed=2450165; DOI=10.1084/jem.167.2.718;
RA Dallo S.F., Su C.-J., Horton J.R., Baseman J.B.;
RT "Identification of P1 gene domain containing epitope(s) mediating
RT Mycoplasma pneumoniae cytoadherence.";
RL J. Exp. Med. 167:718-723(1988).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 29342 / M129;
RX PubMed=11271496;
RX DOI=10.1002/1522-2683(200011)21:17<3765::aid-elps3765>3.0.co;2-6;
RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., Herrmann R.,
RA Frank R.;
RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae.";
RL Electrophoresis 21:3765-3780(2000).
CC -!- FUNCTION: The protein is the major adhesin mediating the attachment of
CC this mycoplasma to respiratory epithelium.
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; M18639; AAA25424.1; -; Genomic_DNA.
DR EMBL; M21519; AAA88325.1; -; Genomic_DNA.
DR EMBL; U00089; AAB95661.1; -; Genomic_DNA.
DR EMBL; X07191; CAB37298.1; -; Genomic_DNA.
DR PIR; A41480; A41480.
DR PIR; S03725; IJYMAP.
DR RefSeq; NP_109829.1; NC_000912.1.
DR RefSeq; WP_010874498.1; NC_000912.1.
DR AlphaFoldDB; P11311; -.
DR SMR; P11311; -.
DR IntAct; P11311; 8.
DR PRIDE; P11311; -.
DR EnsemblBacteria; AAB95661; AAB95661; MPN_141.
DR KEGG; mpn:MPN_141; -.
DR PATRIC; fig|272634.6.peg.155; -.
DR HOGENOM; CLU_251889_0_0_14; -.
DR OMA; EYVPRMA; -.
DR BioCyc; MPNE272634:G1GJ3-237-MON; -.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:AgBase.
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; IPR004940; Adhesin_P1_dom.
DR InterPro; IPR022116; P1_N.
DR Pfam; PF03257; Adhesin_P1; 1.
DR Pfam; PF12378; CytadhesinP1; 1.
DR TIGRFAMs; TIGR03839; termin_org_P1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytadherence; Direct protein sequencing; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..59
FT CHAIN 60..1627
FT /note="Adhesin P1"
FT /id="PRO_0000020629"
FT TRANSMEM 1527..1547
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 219..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1274..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1403..1415
FT /note="Cytadherence epitope"
FT REGION 1589..1627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1336..1362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1603..1627
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1627 AA; 176270 MW; 14F7A2CBA36E6116 CRC64;
MHQTKKTALS KSTWILILTA TASLATGLTV VGHFTSTTTT LKRQQFSYTR PDEVALRHTN
AINPRLTPWT YRNTSFSSLP LTGENPGAWA LVRDNSAKGI TAGSGSQQTT YDPTRTEAAL
TASTTFALRR YDLAGRALYD LDFSKLNPQT PTRDQTGQIT FNPFGGFGLS GAAPQQWNEV
KNKVPVEVAQ DPSNPYRFAV LLVPRSVVYY EQLQRGLGLP QQRTESGQNT STTGAMFGLK
VKNAEADTAK SNEKLQGAEA TGSSTTSGSG QSTQRGGSSG DTKVKALKIE VKKKSDSEDN
GQLQLEKNDL ANAPIKRSEE SGQSVQLKAD DFGTALSSSG SGGNSNPGSP TPWRPWLATE
QIHKDLPKWS ASILILYDAP YARNRTAIDR VDHLDPKAMT ANYPPSWRTP KWNHHGLWDW
KARDVLLQTT GFFNPRRHPE WFDGGQTVAD NEKTGFDVDN SENTKQGFQK EADSDKSAPI
ALPFEAYFAN IGNLTWFGQA LLVFGGNGHV TKSAHTAPLS IGVFRVRYNA TGTSATVTGW
PYALLFSGMV NKQTDGLKDL PFNNNRWFEY VPRMAVAGAK FVGRELVLAG TITMGDTATV
PRLLYDELES NLNLVAQGQG LLREDLQLFT PYGWANRPDL PIGAWSSSSS SSHNAPYYFH
NNPDWQDRPI QNVVDAFIKP WEDKNGKDDA KYIYPYRYSG MWAWQVYNWS NKLTDQPLSA
DFVNENAYQP NSLFAAILNP ELLAALPDKV KYGKENEFAA NEYERFNQKL TVAPTQGTNW
SHFSPTLSRF STGFNLVGSV LDQVLDYVPW IGNGYRYGNN HRGVDDITAP QTSAGSSSGI
STNTSGSRSF LPTFSNIGVG LKANVQATLG GSQTMITGGS PRRTLDQANL QLWTGAGWRN
DKASSGQSDE NHTKFTSATG MDQQGQSGTS AGNPDSLKQD NISKSGDSLT TQDGNAIDQQ
EATNYTNLPP NLTPTADWPN ALSFTNKNNA QRAQLFLRGL LGSIPVLVNR SGSDSNKFQA
TDQKWSYTDL HSDQTKLNLP AYGEVNGLLN PALVETYFGN TRAGGSGSNT TSSPGIGFKI
PEQNNDSKAT LITPGLAWTP QDVGNLVVSG TTVSFQLGGW LVTFTDFVKP RAGYLGLQLT
GLDASDATQR ALIWAPRPWA AFRGSWVNRL GRVESVWDLK GVWADQAQSD SQGSTTTATR
NALPEHPNAL AFQVSVVEAS AYKPNTSSGQ TQSTNSSPYL HLVKPKKVTQ SDKLDDDLKN
LLDPNQVRTK LRQSFGTDHS TQPQPQSLKT TTPVFGTSSG NLSSVLSGGG AGGGSSGSGQ
SGVDLSPVEK VSGWLVGQLP STSDGNTSST NNLAPNTNTG NDVVGVGRLS ESNAAKMNDD
VDGIVRTPLA ELLDGEGQTA DTGPQSVKFK SPDQIDFNRL FTHPVTDLFD PVTMLVYDQY
IPLFIDIPAS VNPKMVRLKV LSFDTNEQSL GLRLEFFKPD QDTQPNNNVQ VNPNNGDFLP
LLTASSQGPQ TLFSPFNQWP DYVLPLAITV PIVVIVLSVT LGLAIGIPMH KNKQALKAGF
ALSNQKVDVL TKAVGSVFKE IINRTGISQA PKRLKQTSAA KPGAPRPPVP PKPGAPKPPV
QPPKKPA
