ID   PANZ_SALTY              Reviewed;         127 AA.
AC   Q7CPJ9;
DT   01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=PanD regulatory factor {ECO:0000255|HAMAP-Rule:MF_02018, ECO:0000305};
GN   Name=panM {ECO:0000303|PubMed:22497218};
GN   Synonyms=panZ {ECO:0000250|UniProtKB:P37613},
GN   yhhK {ECO:0000312|EMBL:AAL22425.1};
GN   OrderedLocusNames=STM3565 {ECO:0000312|EMBL:AAL22425.1};
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   FUNCTION, SUBUNIT, INTERACTION WITH PAND, AND DISRUPTION PHENOTYPE.
RC   STRAIN=LT2;
RX   PubMed=22497218; DOI=10.1111/j.1365-2958.2012.08046.x;
RA   Stuecker T.N., Hodge K.M., Escalante-Semerena J.C.;
RT   "The missing link in coenzyme A biosynthesis: PanM (formerly YhhK), a yeast
RT   GCN5 acetyltransferase homologue triggers aspartate decarboxylase (PanD)
RT   maturation in Salmonella enterica.";
RL   Mol. Microbiol. 84:608-619(2012).
RN   [3]
RP   FUNCTION, INTERACTION WITH PAND, AND MUTAGENESIS OF GLY-76.
RC   STRAIN=LT2;
RX   PubMed=22782525; DOI=10.1128/mbio.00158-12;
RA   Stuecker T.N., Tucker A.C., Escalante-Semerena J.C.;
RT   "PanM, an acetyl-coenzyme A sensor required for maturation of L-aspartate
RT   decarboxylase (PanD).";
RL   MBio 3:76-76(2012).
CC   -!- FUNCTION: Controls both the activation and catalytic activity of PanD
CC       in a coenzyme A (CoA)-dependent fashion (By similarity). Binding of CoA
CC       or a derivative to PanM leads to interaction with PanD, which promotes
CC       the processing and activation of pro-PanD, and subsequent substrate-
CC       mediated inhibition of the active form of PanD (By similarity)
CC       (PubMed:22497218, PubMed:22782525). Lacks acetyltransferase activity
CC       (PubMed:22782525). {ECO:0000250|UniProtKB:P37613,
CC       ECO:0000269|PubMed:22497218, ECO:0000269|PubMed:22782525}.
CC   -!- SUBUNIT: Interacts with PanD in the presence of CoA (PubMed:22497218,
CC       PubMed:22782525). Monomer (PubMed:22497218).
CC       {ECO:0000269|PubMed:22497218, ECO:0000269|PubMed:22782525}.
CC   -!- DISRUPTION PHENOTYPE: Deletion results in a pantothenate auxotrophy.
CC       Deletion mutant accumulates pro-PanD. {ECO:0000269|PubMed:22497218}.
CC   -!- SIMILARITY: Belongs to the PanZ/PanM family. {ECO:0000255|HAMAP-
CC       Rule:MF_02018, ECO:0000305}.
CC   -!- CAUTION: Lacks the conserved catalytic glutamate found in many
CC       enzymatically active members of the Gcn5-like N-acetyltransferase
CC       (GNAT) family. {ECO:0000305|PubMed:22782525}.
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DR   EMBL; AE006468; AAL22425.1; -; Genomic_DNA.
DR   RefSeq; NP_462466.1; NC_003197.2.
DR   RefSeq; WP_000778873.1; NC_003197.2.
DR   AlphaFoldDB; Q7CPJ9; -.
DR   SMR; Q7CPJ9; -.
DR   STRING; 99287.STM3565; -.
DR   PaxDb; Q7CPJ9; -.
DR   EnsemblBacteria; AAL22425; AAL22425; STM3565.
DR   GeneID; 1255088; -.
DR   KEGG; stm:STM3565; -.
DR   PATRIC; fig|99287.12.peg.3768; -.
DR   HOGENOM; CLU_135649_0_0_6; -.
DR   OMA; HFSDQDR; -.
DR   PhylomeDB; Q7CPJ9; -.
DR   BioCyc; SENT99287:STM3565-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0031638; P:zymogen activation; IEA:InterPro.
DR   HAMAP; MF_02018; PanZ_PanM; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR032900; PanZ.
DR   InterPro; IPR040448; PanZ_GNAT.
DR   Pfam; PF12568; PanZ; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   1: Evidence at protein level;
KW   Pantothenate biosynthesis; Reference proteome.
FT   CHAIN           1..127
FT                   /note="PanD regulatory factor"
FT                   /id="PRO_0000432590"
FT   DOMAIN          1..127
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02018"
FT   BINDING         66..68
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02018"
FT   BINDING         72..79
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02018"
FT   MUTAGEN         76
FT                   /note="G->L: Loss of activity. Cannot bind acetyl-CoA. Does
FT                   not interact with pro-PanD."
FT                   /evidence="ECO:0000269|PubMed:22782525"
SQ   SEQUENCE   127 AA;  14480 MW;  6E66F2F879BFC959 CRC64;
     MKLTILRLEH FSAQDQIDLG KIWPEYSASS LSVDETHRIY AARFNERLLG AVRVTLSGTQ
     GALDSLRVRE ITRRRGVGQY LVEEVIRDNP NVSSWWMADV GVEDRSVMAA FMQALGFTAQ
     HDGWEKR