P30_MYCPN
ID P30_MYCPN Reviewed; 274 AA.
AC P75330; P94960; Q50282;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=P30 adhesin;
DE AltName: Full=30 kDa adhesin-related protein;
DE AltName: Full=Cytadhesin P30;
GN Name=p30; OrderedLocusNames=MPN_453; ORFNames=MP388;
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].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=2123834; DOI=10.1128/iai.58.12.4163-4165.1990;
RA Dallo S.F., Chavoya A., Baseman J.B.;
RT "Characterization of the gene for a 30-kilodalton adhesion-related protein
RT of Mycoplasma pneumoniae.";
RL Infect. Immun. 58:4163-4165(1990).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129 mutant M6;
RX PubMed=7836325; DOI=10.1128/jb.177.3.843-846.1995;
RA Layh-Schmitt G., Hilbert H., Pirkl E.;
RT "A spontaneous hemadsorption-negative mutant of Mycoplasma pneumoniae
RT exhibits a truncated adhesin-related 30-kilodalton protein and lacks the
RT cytadherence-accessory protein HMW1.";
RL J. Bacteriol. 177:843-846(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129 mutant M7;
RA Layh-Schmitt G., Himmelreich R., Leibfried U.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Adhesin necessary for successful cytadherence and virulence.
CC -!- SUBCELLULAR LOCATION: Cell projection, attachment organelle membrane;
CC Multi-pass membrane protein. Note=Integral and surface exposed membrane
CC protein that localizes to the membrane at the attachment organelle.
CC -!- DOMAIN: 13 hexapeptides with consensus sequence were found at the
CC carboxy end between AA 177 and 267 in a proline-rich domain.
CC -!- MISCELLANEOUS: Spontaneous hemadsorption-negative mutants M6 and M7
CC exhibit a truncated P30 adhesin.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M57245; AAB36603.1; -; Genomic_DNA.
DR EMBL; U00089; AAB96036.1; -; Genomic_DNA.
DR EMBL; Z46228; CAB56613.1; -; Genomic_DNA.
DR EMBL; U30326; AAC45467.1; -; Genomic_DNA.
DR PIR; A41461; A41461.
DR RefSeq; NP_110141.1; NC_000912.1.
DR RefSeq; WP_010874809.1; NC_000912.1.
DR AlphaFoldDB; P75330; -.
DR IntAct; P75330; 1.
DR STRING; 272634.MPN_453; -.
DR EnsemblBacteria; AAB96036; AAB96036; MPN_453.
DR KEGG; mpn:MPN_453; -.
DR PATRIC; fig|272634.6.peg.489; -.
DR HOGENOM; CLU_086637_0_0_14; -.
DR OMA; NNFNPRM; -.
DR BioCyc; MPNE272634:G1GJ3-733-MON; -.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0033111; C:attachment organelle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0020035; P:adhesion of symbiont to microvasculature; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR InterPro; IPR009896; Cytadhesin_P30/P32.
DR Pfam; PF07271; Cytadhesin_P30; 1.
PE 4: Predicted;
KW Cell adhesion; Cell membrane; Cell projection; Cytadherence; Lipoprotein;
KW Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix;
KW Virulence.
FT CHAIN 1..274
FT /note="P30 adhesin"
FT /id="PRO_0000058130"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 177..182
FT /note="1-1"
FT REPEAT 183..188
FT /note="2-1"
FT REPEAT 189..194
FT /note="1-2"
FT REPEAT 195..200
FT /note="3-1"
FT REPEAT 201..206
FT /note="1-3"
FT REPEAT 207..212
FT /note="2-2"
FT REPEAT 213..218
FT /note="1-4"
FT REPEAT 219..224
FT /note="3-2"
FT REPEAT 225..230
FT /note="1-5"
FT REPEAT 231..236
FT /note="2-3"
FT REPEAT 237..242
FT /note="1-6"
FT REPEAT 243..248
FT /note="3-3"
FT REPEAT 249..254
FT /note="1-7"
FT REPEAT 268..273
FT /note="3-4"
FT REGION 128..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..254
FT /note="7 X 6 AA repeats of P-G-M-A-P-R"
FT REGION 183..236
FT /note="3 X 6 AA repeats of P-G-M-P-P-H"
FT REGION 195..248
FT /note="4 X 6 AA repeats of P-G-F-P-P-Q"
FT COMPBIAS 174..274
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 186..257
FT /note="Missing (in strain: mutant M7)"
FT VARIANT 210..257
FT /note="Missing (in strain: mutant M6)"
FT CONFLICT 80
FT /note="G -> V (in Ref. 1; AAB36603)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 274 AA; 29741 MW; BFB047831A4C9D7D CRC64;
MKLPPRRKLK LFLLAWMLVL FSALIVLATL ILVQHNNTEL TEVKSELSPL NVVLHAEEDT
VQIQGKPITE QAWFIPTVAG CFGFSALAII LGLAIGLPIV KRKEKRLLEE KERQEQLAEQ
LQRISAQQEE QQALEQQAAA EAHAEAEVEP APQPVPVPPQ PQVQINFGPR TGFPPQPGMA
PRPGMPPHPG MAPRPGFPPQ PGMAPRPGMP PHPGMAPRPG FPPQPGMAPR PGMPPHPGMA
PRPGFPPQPG MAPRPGMQPP RPGMPPQPGF PPKR
