REDM_STRCO
ID REDM_STRCO Reviewed; 532 AA.
AC O54154;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=L-proline--[L-prolyl-carrier protein] ligase {ECO:0000305};
DE EC=6.2.1.53 {ECO:0000269|PubMed:11880032};
DE AltName: Full=L-prolyl-AMP ligase {ECO:0000303|PubMed:11880032};
GN Name=redM {ECO:0000303|PubMed:11514230};
GN OrderedLocusNames=SCO5891 {ECO:0000312|EMBL:CAA16182.1};
GN ORFNames=FHV98_107150;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A3(2) / ICSSB 1010;
RA Yuzawa S.;
RT "Genome sequencing of Streptomyces strains engineered using actinophage
RT integration system.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP GENE CLUSTER, AND FUNCTION.
RX PubMed=11514230; DOI=10.1016/s1074-5521(01)00054-0;
RA Cerdeno A.M., Bibb M.J., Challis G.L.;
RT "Analysis of the prodiginine biosynthesis gene cluster of Streptomyces
RT coelicolor A3(2): new mechanisms for chain initiation and termination in
RT modular multienzymes.";
RL Chem. Biol. 8:817-829(2001).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11880032; DOI=10.1016/s1074-5521(02)00100-x;
RA Thomas M.G., Burkart M.D., Walsh C.T.;
RT "Conversion of L-proline to pyrrolyl-2-carboxyl-S-PCP during
RT undecylprodigiosin and pyoluteorin biosynthesis.";
RL Chem. Biol. 9:171-184(2002).
CC -!- FUNCTION: Involved in the biosynthesis of undecylprodigiosin
CC (PubMed:11514230, PubMed:11880032). Catalyzes the conversion of L-
CC proline to L-prolyl-AMP and the transfer of the L-prolyl group to acyl
CC carrier protein RedO (PubMed:11880032). {ECO:0000269|PubMed:11514230,
CC ECO:0000269|PubMed:11880032}.
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:11880032};
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AL939125; CAA16182.1; -; Genomic_DNA.
DR EMBL; VNID01000007; TYP13356.1; -; Genomic_DNA.
DR PIR; T34917; T34917.
DR RefSeq; NP_630012.1; NC_003888.3.
DR RefSeq; WP_011030516.1; NZ_VNID01000007.1.
DR AlphaFoldDB; O54154; -.
DR SMR; O54154; -.
DR STRING; 100226.SCO5891; -.
DR GeneID; 1101333; -.
DR KEGG; sco:SCO5891; -.
DR PATRIC; fig|100226.15.peg.5990; -.
DR eggNOG; COG1020; Bacteria.
DR HOGENOM; CLU_000022_2_12_11; -.
DR InParanoid; O54154; -.
DR OMA; RTLYPIG; -.
DR PhylomeDB; O54154; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000036; F:acyl carrier activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IBA:GO_Central.
DR CDD; cd05945; DltA; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
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 InterPro; IPR044507; DltA-like.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..532
FT /note="L-proline--[L-prolyl-carrier protein] ligase"
FT /id="PRO_0000448664"
FT REGION 510..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 532 AA; 56886 MW; FCA459F5CBDE24C0 CRC64;
MSAATPSVIR LPRDTSAQHA ARPAFVGSDP LTYGEFTARV EAVAARLLSL GTRTGDRIAV
WMDKQPRYAE AIVAALEAGC AYVPLDGGQP VSRVRTILAD AEPVVLFTDA HHAALLGDDD
LPASVTTVVA VGDALPDTVG GIPVAPWESW EQGRAGRVTL LPSLTPGDLA ALLYTSGSTG
TPKGVQISHG ALANFVAWAR DELDVGPDDV FAGHASFNFD LSTFDLFTAL SCGAAVWIVP
DAATKDVTAL AEGIRRHRIT VWYSVPSVLH LLTTSAALTP EHAASLRYVL FAGEVFPVPQ
LRALRELLPP GTPLYNLYGP TETNVCTYHR VRPEDLHRAT PVPIGLPITG AGTTVVDDAG
RTVREPGAIG ELHVSGVCVT PGYWRRAEEP VSTAHCRGVH PTGDLVSYEE DGRLVYRGRK
DRMVKLSGYR VELGEIEAAA LRHPGIAEAA VLVDGSGPKA RLRLYYTLCE GAERIGLVEL
KQHCARHLPT YMVPHGAVRL DRMPLNPNGK TDYRRLGLDA PPRPAAPLGT AR
