ID   PIGI_SERS3              Reviewed;         491 AA.
AC   Q5W263;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=L-proline--[L-prolyl-carrier protein] ligase {ECO:0000305};
DE            EC=6.2.1.53 {ECO:0000269|PubMed:17002325};
DE   AltName: Full=L-prolyl-AMP ligase {ECO:0000303|PubMed:17002325};
GN   Name=pigI {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, CATALYTIC ACTIVITY, 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) (PubMed:15853884,
CC       PubMed:17002325). Catalyzes the conversion of L-proline to L-prolyl-AMP
CC       and the transfer of the L-prolyl group to acyl carrier protein PigG
CC       (PubMed:17002325). {ECO:0000269|PubMed:15853884,
CC       ECO:0000269|PubMed:17002325}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + holo-[peptidyl-carrier protein] + L-proline = AMP +
CC         diphosphate + L-prolyl-[peptidyl-carrier protein];
CC         Xref=Rhea:RHEA:11656, Rhea:RHEA-COMP:11480, Rhea:RHEA-COMP:14109,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:60039,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:138622, ChEBI:CHEBI:456215;
CC         EC=6.2.1.53; Evidence={ECO:0000269|PubMed:17002325};
CC   -!- PATHWAY: Antibiotic biosynthesis; prodigiosin biosynthesis.
CC       {ECO:0000269|PubMed:15853884, ECO:0000269|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}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AJ833001; CAH55637.1; -; Genomic_DNA.
DR   RefSeq; WP_021014647.1; NZ_CP025085.1.
DR   AlphaFoldDB; Q5W263; -.
DR   SMR; Q5W263; -.
DR   STRING; 104623.Ser39006_01377; -.
DR   PRIDE; Q5W263; -.
DR   KEGG; ag:CAH55637; -.
DR   eggNOG; COG1020; Bacteria.
DR   OrthoDB; 377638at2; -.
DR   BRENDA; 6.2.1.53; 15756.
DR   UniPathway; UPA01072; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IMP:UniProtKB.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; ATP-binding; Ligase; Nucleotide-binding.
FT   CHAIN           1..491
FT                   /note="L-proline--[L-prolyl-carrier protein] ligase"
FT                   /id="PRO_0000436245"
SQ   SEQUENCE   491 AA;  53701 MW;  AB99D957D31FE475 CRC64;
     MTISTPVIID SLIRHAQRTP EQTALLCGDQ HWNYRQLVTR AHVMASALRQ AGLSGQAILL
     NLPKSLDAVA AIYATWLSGN HYIPIDYSQP SSRIERIIAA AAPALIIDTA WLATLDSQPS
     FDAEQPVGRM VYHNPIAAIL YTSGSTGTPK GVQISHEMLG FFIQWAVRDT QLTARDVLSN
     HASFAFDLST FDLFASAYVG AATWIIRESE QKDCAALAQG LQRHAVSVWY SVPSILAMLE
     KSTLLNPTLG QSLRQVIFAG EPYPVTALKR LLPCLPQPCR VSNWYGPTET NVCVAYAIDR
     ARLAMLKQVP IGLPLEGLTA QLEDENGDRH PLTAQLRLSG ELLISGPCVT PGYSNVVVPR
     QAALHPHQCH ATGDWVEMTP EGLVFRGRID DMVKINGYRV ELGEIESVLH QHPAIDRAAL
     CVELGDLRQT LIMVISLQTG AVPPGLLELK QFLQQKLPSY MIPNKLVITE SLPVNANGKV
     DRKQLAGVVA V