COAD_STAAW
ID COAD_STAAW Reviewed; 160 AA.
AC P63820; Q99UX9;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000303|PubMed:24041904};
DE EC=2.7.7.3 {ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:24041904};
DE AltName: Full=Dephospho-CoA pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00151};
DE AltName: Full=Pantetheine-phosphate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00151};
DE Short=PPAT {ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000303|PubMed:24041904};
GN Name=coaD {ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000303|PubMed:24041904};
GN OrderedLocusNames=MW1007;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEXES WITH SEVERAL CYCLOALKYL
RP PYRIMIDINE INHIBITORS; ADP AND ATP ANALOG, FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, BIOTECHNOLOGY, AND SUBUNIT.
RX PubMed=24041904; DOI=10.1128/aac.01661-13;
RA de Jonge B.L., Walkup G.K., Lahiri S.D., Huynh H., Neckermann G., Utley L.,
RA Nash T.J., Brock J., San Martin M., Kutschke A., Johnstone M., Laganas V.,
RA Hajec L., Gu R.F., Ni H., Chen B., Hutchings K., Holt E., McKinney D.,
RA Gao N., Livchak S., Thresher J.;
RT "Discovery of inhibitors of 4'-phosphopantetheine adenylyltransferase
RT (PPAT) to validate PPAT as a target for antibacterial therapy.";
RL Antimicrob. Agents Chemother. 57:6005-6015(2013).
CC -!- FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-
CC phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
CC {ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:24041904}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA +
CC diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328,
CC ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00151, ECO:0000269|PubMed:24041904};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00151};
CC -!- ACTIVITY REGULATION: Is inhibited by a series of cycloalkyl
CC pyrimidines, which also show suppression of bacterial growth.
CC {ECO:0000269|PubMed:24041904}.
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00151}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00151,
CC ECO:0000305|PubMed:24041904}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00151}.
CC -!- BIOTECHNOLOGY: PPAT is a validated novel target for antibacterial
CC therapy against Gram-positive bacteria. {ECO:0000269|PubMed:24041904}.
CC -!- SIMILARITY: Belongs to the bacterial CoaD family. {ECO:0000255|HAMAP-
CC Rule:MF_00151}.
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DR EMBL; BA000033; BAB94872.1; -; Genomic_DNA.
DR RefSeq; WP_000401377.1; NC_003923.1.
DR PDB; 4NAH; X-ray; 2.38 A; A/B/C/D/E/F=1-160.
DR PDB; 4NAT; X-ray; 1.72 A; A/B/C=1-160.
DR PDB; 4NAU; X-ray; 2.33 A; A/B/C=1-160.
DR PDBsum; 4NAH; -.
DR PDBsum; 4NAT; -.
DR PDBsum; 4NAU; -.
DR AlphaFoldDB; P63820; -.
DR SMR; P63820; -.
DR EnsemblBacteria; BAB94872; BAB94872; BAB94872.
DR GeneID; 66839319; -.
DR KEGG; sam:MW1007; -.
DR HOGENOM; CLU_100149_0_1_9; -.
DR OMA; EFQMALM; -.
DR UniPathway; UPA00241; UER00355.
DR EvolutionaryTrace; P63820; -.
DR Proteomes; UP000000418; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004595; F:pantetheine-phosphate adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02163; PPAT; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00151; PPAT_bact; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR001980; PPAT.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR21342:SF1; PTHR21342:SF1; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR PRINTS; PR01020; LPSBIOSNTHSS.
DR TIGRFAMs; TIGR01510; coaD_prev_kdtB; 1.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Magnesium;
KW Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT CHAIN 1..160
FT /note="Phosphopantetheine adenylyltransferase"
FT /id="PRO_0000156276"
FT BINDING 11..12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT ECO:0000305|PubMed:24041904, ECO:0007744|PDB:4NAT,
FT ECO:0007744|PDB:4NAU"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT ECO:0000305|PubMed:24041904, ECO:0007744|PDB:4NAU"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 90..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT ECO:0000305|PubMed:24041904, ECO:0007744|PDB:4NAT,
FT ECO:0007744|PDB:4NAU"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT ECO:0000305|PubMed:24041904, ECO:0007744|PDB:4NAH"
FT BINDING 121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:24041904,
FT ECO:0007744|PDB:4NAH, ECO:0007744|PDB:4NAU"
FT BINDING 125..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT ECO:0000305|PubMed:24041904, ECO:0007744|PDB:4NAU"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:4NAT"
FT HELIX 17..26
FT /evidence="ECO:0007829|PDB:4NAT"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:4NAT"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:4NAT"
FT HELIX 49..59
FT /evidence="ECO:0007829|PDB:4NAT"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:4NAT"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:4NAT"
FT HELIX 75..82
FT /evidence="ECO:0007829|PDB:4NAT"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:4NAT"
FT HELIX 94..110
FT /evidence="ECO:0007829|PDB:4NAT"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:4NAT"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:4NAT"
FT HELIX 130..138
FT /evidence="ECO:0007829|PDB:4NAT"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:4NAT"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:4NAT"
SQ SEQUENCE 160 AA; 18371 MW; 67B4E6F42DBC8D41 CRC64;
MEHTIAVIPG SFDPITYGHL DIIERSTDRF DEIHVCVLKN SKKEGTFSLE ERMDLIEQSV
KHLPNVKVHQ FSGLLVDYCE QVGAKTIIRG LRAVSDFEYE LRLTSMNKKL NNEIETLYMM
SSTNYSFISS SIVKEVAAYR ADISEFVPPY VEKALKKKFK
