SWISSPROT: A0A0H2Y4P1_YERPA

ID   A0A0H2Y4P1_YERPA        Unreviewed;       145 AA.
AC   A0A0H2Y4P1;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   08-MAY-2019, entry version 21.
DE   RecName: Full=PanD regulatory factor {ECO:0000256|HAMAP-Rule:MF_02018};
GN   Name=panZ {ECO:0000256|HAMAP-Rule:MF_02018};
GN   OrderedLocusNames=YPA_0213 {ECO:0000313|EMBL:ABG12182.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12182.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12182.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12182.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- FUNCTION: Controls both the activation and catalytic activity of
CC       PanD in a coenzyme A (CoA)-dependent fashion. {ECO:0000256|HAMAP-
CC       Rule:MF_02018}.
CC   -!- SUBUNIT: Interacts with PanD in the presence of CoA.
CC       {ECO:0000256|HAMAP-Rule:MF_02018}.
CC   -!- SIMILARITY: Belongs to the PanZ/PanM family. {ECO:0000256|HAMAP-
CC       Rule:MF_02018}.
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DR   EMBL; CP000308; ABG12182.1; -; Genomic_DNA.
DR   EnsemblBacteria; ABG12182; ABG12182; YPA_0213.
DR   KEGG; ypa:YPA_0213; -.
DR   OMA; RGVMAAF; -.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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   3: Inferred from homology;
DR   PRODOM; A0A0H2Y4P1.
DR   SWISS-2DPAGE; A0A0H2Y4P1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Pantothenate biosynthesis {ECO:0000256|HAMAP-Rule:MF_02018};
KW   Transferase {ECO:0000313|EMBL:ABG12182.1}.
FT   DOMAIN       21    145       N-acetyltransferase.
FT                                {ECO:0000259|PROSITE:PS51186}.
FT   REGION       83     85       Coenzyme A binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_02018}.
FT   REGION       89     96       Coenzyme A binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_02018}.
SQ   SEQUENCE   145 AA;  16742 MW;  5560601B4AA846DC CRC64;
     MNLGAISTLL LWLLAMKLTI ERLITLTHQD VIDLAKIWPN QQPAAWQQWI TEGRPLFAAR
     FNERLLGAVK VAVYDQQAEL QDLCVREVTR RRGVGLYLIE ETLRQLPEIK HWYLNGGDLT
     AAERPQMNSF MLACGFSHEA QGWRR
//