PIGG_SERS3
ID PIGG_SERS3 Reviewed; 87 AA.
AC Q5W265;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=Probable acyl carrier protein PigG {ECO:0000303|PubMed:17002325};
DE AltName: Full=Peptidyl carrier protein {ECO:0000303|PubMed:17002325};
DE Short=PCP {ECO:0000303|PubMed:17002325};
GN Name=pigG {ECO:0000303|PubMed:15528645};
OS Serratia sp. (strain ATCC 39006).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia; unclassified Serratia.
OX NCBI_TaxID=104623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 39006 / SC 11482;
RX PubMed=15528645; DOI=10.1099/mic.0.27222-0;
RA Harris A.K., Williamson N.R., Slater H., Cox A., Abbasi S., Foulds I.,
RA Simonsen H.T., Leeper F.J., Salmond G.P.;
RT "The Serratia gene cluster encoding biosynthesis of the red antibiotic,
RT prodigiosin, shows species- and strain-dependent genome context
RT variation.";
RL Microbiology 150:3547-3560(2004).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=ATCC 39006 / SC 11482;
RX PubMed=15853884; DOI=10.1111/j.1365-2958.2005.04602.x;
RA Williamson N.R., Simonsen H.T., Ahmed R.A., Goldet G., Slater H.,
RA Woodley L., Leeper F.J., Salmond G.P.;
RT "Biosynthesis of the red antibiotic, prodigiosin, in Serratia:
RT identification of a novel 2-methyl-3-n-amyl-pyrrole (MAP) assembly pathway,
RT definition of the terminal condensing enzyme, and implications for
RT undecylprodigiosin biosynthesis in Streptomyces.";
RL Mol. Microbiol. 56:971-989(2005).
RN [3]
RP FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 39006 / SC 11482;
RX PubMed=17002325; DOI=10.1021/ja063611l;
RA Garneau-Tsodikova S., Dorrestein P.C., Kelleher N.L., Walsh C.T.;
RT "Protein assembly line components in prodigiosin biosynthesis:
RT characterization of PigA,G,H,I,J.";
RL J. Am. Chem. Soc. 128:12600-12601(2006).
CC -!- FUNCTION: Involved in the biosynthesis of 4-methoxy-2,2'-bipyrrole-5-
CC carbaldehyde (MBC), one of the terminal products involved in the
CC biosynthesis of the red antibiotic prodigiosin (Pig). Carrier of the L-
CC prolyl group transferred from L-prolyl-AMP by PigI.
CC {ECO:0000269|PubMed:15853884, ECO:0000269|PubMed:17002325}.
CC -!- PATHWAY: Antibiotic biosynthesis; prodigiosin biosynthesis.
CC {ECO:0000305|PubMed:15853884, ECO:0000305|PubMed:17002325}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a white phenotype
CC and produce 2-methyl-3-n-amyl-pyrrole (MAP).
CC {ECO:0000269|PubMed:15853884}.
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DR EMBL; AJ833001; CAH55635.1; -; Genomic_DNA.
DR RefSeq; WP_021014645.1; NZ_CP025085.1.
DR PDB; 5JDX; NMR; -; A=1-87.
DR PDBsum; 5JDX; -.
DR AlphaFoldDB; Q5W265; -.
DR BMRB; Q5W265; -.
DR SMR; Q5W265; -.
DR STRING; 104623.Ser39006_01375; -.
DR KEGG; ag:CAH55635; -.
DR eggNOG; COG0236; Bacteria.
DR OrthoDB; 1943389at2; -.
DR UniPathway; UPA01072; -.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IMP:UniProtKB.
DR Gene3D; 1.10.1200.10; -; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR SUPFAM; SSF47336; SSF47336; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Phosphopantetheine; Phosphoprotein.
FT CHAIN 1..87
FT /note="Probable acyl carrier protein PigG"
FT /id="PRO_0000436244"
FT DOMAIN 1..78
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 36
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000250|UniProtKB:P0A2W5,
FT ECO:0000255|PROSITE-ProRule:PRU00258"
FT HELIX 2..15
FT /evidence="ECO:0007829|PDB:5JDX"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:5JDX"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:5JDX"
FT HELIX 36..49
FT /evidence="ECO:0007829|PDB:5JDX"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:5JDX"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:5JDX"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:5JDX"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:5JDX"
SQ SEQUENCE 87 AA; 9536 MW; F4A8EDA4E31DDF49 CRC64;
MLESKLINHI ATQFLDGEKD GLDSQTPLFE LNIVDSAAIF DLVDFLRQES KVSIGMQEIH
PANFATVQSM VALVQRLKAH PEQGGAA