CARDS_MYCPN
ID CARDS_MYCPN Reviewed; 591 AA.
AC P75409; Q1PD42; Q1PD43; Q1PD44; Q1PD45; Q1PD46;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=ADP-ribosylating toxin CARDS;
DE EC=2.4.2.-;
DE AltName: Full=ADP-ribosyltransferase CARDS;
DE AltName: Full=CARDX TX;
GN OrderedLocusNames=MPN_372; ORFNames=MP464;
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], FUNCTION, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF GLU-132.
RC STRAIN=ATCC 29342 / M129, JL, L2, RJL1, and S1;
RX PubMed=16617115; DOI=10.1073/pnas.0510644103;
RA Kannan T.R., Baseman J.B.;
RT "ADP-ribosylating and vacuolating cytotoxin of Mycoplasma pneumoniae
RT represents unique virulence determinant among bacterial pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6724-6729(2006).
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 IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH HUMAN SFTPA.
RC STRAIN=B9, and S1;
RX PubMed=15845487; DOI=10.1128/iai.73.5.2828-2834.2005;
RA Kannan T.R., Provenzano D., Wright J.R., Baseman J.B.;
RT "Identification and characterization of human surfactant protein A binding
RT protein of Mycoplasma pneumoniae.";
RL Infect. Immun. 73:2828-2834(2005).
CC -!- FUNCTION: Acts as an ADP-ribosylating toxin, which may transfer the
CC ADP-ribosyl group from NAD(+) to specific amino acids in target
CC proteins. Elicits cytopathic effects in mammalian cells, such as
CC disorganization and disruption of respiratory epithelial integrity in
CC tracheal epithelium and vacuolization in the cytoplasm of CHO and HeLa
CC cells. {ECO:0000269|PubMed:16617115}.
CC -!- SUBUNIT: Binds to the pulmonary surfactant-associated protein A
CC (SFTPA/SP-A), the major mammalian protein component of pulmonary
CC surfactant.
CC -!- INTERACTION:
CC P75409; P07355: ANXA2; Xeno; NbExp=6; IntAct=EBI-2259548, EBI-352622;
CC P75409; Q8IWL2: SFTPA1; Xeno; NbExp=2; IntAct=EBI-2259548, EBI-11316418;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16617115};
CC Peripheral membrane protein {ECO:0000269|PubMed:16617115};
CC Extracellular side {ECO:0000269|PubMed:16617115}. Note=Surface-
CC associated protein.
CC -!- SIMILARITY: Belongs to the bacterial exotoxin subunit A family.
CC {ECO:0000305}.
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DR EMBL; DQ447746; ABE27142.1; -; Genomic_DNA.
DR EMBL; DQ447747; ABE27143.1; -; Genomic_DNA.
DR EMBL; DQ447748; ABE27144.1; -; Genomic_DNA.
DR EMBL; DQ447749; ABE27145.1; -; Genomic_DNA.
DR EMBL; DQ447750; ABE27146.1; -; Genomic_DNA.
DR EMBL; U00089; AAB96112.1; -; Genomic_DNA.
DR PIR; S73790; S73790.
DR RefSeq; NP_110060.1; NC_000912.1.
DR RefSeq; WP_010874728.1; NC_000912.1.
DR PDB; 4TLV; X-ray; 1.90 A; A/B/C/D/E/F=1-591.
DR PDB; 4TLW; X-ray; 2.55 A; A=1-591.
DR PDBsum; 4TLV; -.
DR PDBsum; 4TLW; -.
DR AlphaFoldDB; P75409; -.
DR SMR; P75409; -.
DR IntAct; P75409; 2.
DR STRING; 272634.MPN_372; -.
DR EnsemblBacteria; AAB96112; AAB96112; MPN_372.
DR KEGG; mpn:MPN_372; -.
DR PATRIC; fig|272634.6.peg.403; -.
DR HOGENOM; CLU_423249_0_0_14; -.
DR OMA; DECTTHA; -.
DR BioCyc; MPNE272634:G1GJ3-586-MON; -.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0009986; C:cell surface; IDA:AgBase.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0044075; P:modulation by symbiont of host vacuole organization; IMP:AgBase.
DR InterPro; IPR003898; Borpert_toxA.
DR Pfam; PF02917; Pertussis_S1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Glycosyltransferase; Membrane;
KW Reference proteome; Toxin; Transferase; Virulence.
FT CHAIN 1..591
FT /note="ADP-ribosylating toxin CARDS"
FT /id="PRO_0000210665"
FT VARIANT 38
FT /note="L -> P (in strain: S1)"
FT VARIANT 245
FT /note="D -> G (in strain: L2)"
FT VARIANT 308
FT /note="S -> P (in strain: S1)"
FT VARIANT 371
FT /note="I -> S (in strain: S1, L2, RJL1 and JL)"
FT VARIANT 391
FT /note="F -> S (in strain: S1)"
FT VARIANT 392
FT /note="W -> R (in strain: RJL1)"
FT MUTAGEN 132
FT /note="E->A: Reduces ADP-ribosylation activity. Unable to
FT elicit vacuolization in CHO cells at 5 ug/ml."
FT /evidence="ECO:0000269|PubMed:16617115"
FT STRAND 7..14
FT /evidence="ECO:0007829|PDB:4TLV"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:4TLV"
FT HELIX 33..38
FT /evidence="ECO:0007829|PDB:4TLV"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:4TLV"
FT HELIX 54..58
FT /evidence="ECO:0007829|PDB:4TLV"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 74..82
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:4TLV"
FT HELIX 90..102
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:4TLV"
FT HELIX 113..124
FT /evidence="ECO:0007829|PDB:4TLV"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:4TLV"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:4TLV"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 144..156
FT /evidence="ECO:0007829|PDB:4TLV"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:4TLV"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:4TLV"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:4TLV"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 249..256
FT /evidence="ECO:0007829|PDB:4TLV"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:4TLV"
FT HELIX 265..269
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:4TLV"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:4TLV"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 323..327
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 335..340
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 348..354
FT /evidence="ECO:0007829|PDB:4TLV"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 364..368
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 375..380
FT /evidence="ECO:0007829|PDB:4TLV"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 388..393
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:4TLW"
FT STRAND 404..410
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 415..423
FT /evidence="ECO:0007829|PDB:4TLV"
FT HELIX 429..432
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 447..450
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 453..457
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 463..466
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 472..476
FT /evidence="ECO:0007829|PDB:4TLV"
FT TURN 477..479
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 481..487
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 490..495
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 502..508
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 510..512
FT /evidence="ECO:0007829|PDB:4TLV"
FT HELIX 522..524
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 525..529
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 543..548
FT /evidence="ECO:0007829|PDB:4TLV"
FT TURN 549..551
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 554..558
FT /evidence="ECO:0007829|PDB:4TLV"
FT TURN 562..565
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 567..571
FT /evidence="ECO:0007829|PDB:4TLV"
FT STRAND 576..579
FT /evidence="ECO:0007829|PDB:4TLV"
FT TURN 586..589
FT /evidence="ECO:0007829|PDB:4TLV"
SQ SEQUENCE 591 AA; 68057 MW; B958C85C9EE29E90 CRC64;
MPNPVRFVYR VDLRSPEEIF EHGFSTLGDV RNFFEHILST NFGRSYFIST SETPTAAIRF
FGSWLREYVP EHPRRAYLYE IRADQHFYNA RATGENLLDL MRQRQVVFDS GDREMAQMGI
RALRTSFAYQ REWFTDGPIA AANVRSAWLV DAVPVEPGHA HHPAGRVVET TRINEPEMHN
PHYQELQTQA NDQPWLPTPG IATPVHLSIP QAASVADVSE GTSASLSFAC PDWSPPSSNG
ENPLDKCIAE KIDNYNLQSL PQYASSVKEL EDTPVYLRGI KTQKTFMLQA DPQNNNVFLV
EVNPKQKSSF PQTIFFWDVY QRICLKDLTG AQISLSLTAF TTQYAGQLKV HLSVSAVNAV
NQKWKMTPQD IAITQFRVSS ELLGQTENGL FWNTKSGGSQ HDLYVCPLKN PPSDLEELQI
IVDECTTHAQ FVTMRAASTF FVDVQLGWYW RGYYYTPQLS GWSYQMKTPD GQIFYDLKTS
KIFFVQDNQN VFFLHNKLNK QTGYSWDWVE WLKHDMNEDK DENFKWYFSR DDLTIPSVEG
LNFRHIRCYA DNQQLKVIIS GSRWGGWYST YDKVESNVED KILVKDGFDR F
