ID O88027_STRCO Unreviewed; 388 AA.
AC O88027;
DT 01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1998, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN OrderedLocusNames=SCO6671 {ECO:0000313|EMBL:CAA19950.1};
GN ORFNames=SC5A7.21c {ECO:0000313|EMBL:CAA19950.1};
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226 {ECO:0000313|EMBL:CAA19950.1, ECO:0000313|Proteomes:UP000001973};
RN [1] {ECO:0000313|EMBL:CAA19950.1, ECO:0000313|Proteomes:UP000001973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145
RC {ECO:0000313|Proteomes:UP000001973};
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., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J., 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).
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DR EMBL; AL939128; CAA19950.1; -; Genomic_DNA.
DR PIR; T35170; T35170.
DR RefSeq; NP_630746.1; NC_003888.3.
DR RefSeq; WP_011031094.1; NZ_VNID01000002.1.
DR AlphaFoldDB; O88027; -.
DR STRING; 100226.gene:17764329; -.
DR PaxDb; 100226-SCO6671; -.
DR PATRIC; fig|100226.15.peg.6777; -.
DR eggNOG; COG0189; Bacteria.
DR HOGENOM; CLU_052967_3_0_11; -.
DR InParanoid; O88027; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR011226; ATP-grasp_fam.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR PANTHER; PTHR23132:SF0; D-ALANINE-D-ALANINE LIGASE FAMILY; 1.
DR Pfam; PF15632; ATPgrasp_Ter; 1.
DR PIRSF; PIRSF029120; UCP029120; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000001973}.
FT DOMAIN 121..313
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 350..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 388 AA; 41612 MW; 6AB0AA06928D27AC CRC64;
MASPVRVWLN RTYAENVFFM DQLRRNPADR AVEIHATHGD PDSPVLAAAD TAELEPEGLS
PAGYVEYALA QCARRGIDVF VPRLHQSAIV AHRAEFEALG TALLAPPPEA VAVFRDKVIA
YEAVRAIGVP VPPWWRVRTA DELVLAVEEL EAGGHRACFK PASGAGGVGF RMVTRDPFSL
THLNGFPSPS VPLPLVVEAL RAAEEPVDWL VMPRLEQPEV SVDCLTGPDN RVRLAVGRTK
NGRRRGFTLH DQWLTPARRI AETFGLHHLS NVQFRMYGDR PVLMDVNTRP AGGLHQLALC
GVNVPWAAVR LALGDDPGQL EPPFLGQDYA VVSGPRPLRP VTLPHQRADL PAATTPAPAP
APAAAAAPAP APAERAAAPA SSAPVGLT
//
