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Database: UniProt
Entry: A0A398AQ37_BRACM
LinkDB: A0A398AQ37_BRACM
Original site: A0A398AQ37_BRACM 
ID   A0A398AQ37_BRACM        Unreviewed;       949 AA.
AC   A0A398AQ37;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN   ORFNames=BRARA_A02500 {ECO:0000313|EMBL:RID79791.1};
OS   Brassica campestris (Field mustard).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3711 {ECO:0000313|EMBL:RID79791.1, ECO:0000313|Proteomes:UP000264353};
RN   [1] {ECO:0000313|EMBL:RID79791.1, ECO:0000313|Proteomes:UP000264353}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B-3 {ECO:0000313|Proteomes:UP000264353};
RA   Bowman J., Kohchi T., Yamato K., Jenkins J., Shu S., Ishizaki K.,
RA   Yamaoka S., Nishihama R., Nakamura Y., Berger F., Adam C., Aki S.,
RA   Althoff F., Araki T., Arteaga-Vazquez M., Balasubrmanian S., Bauer D.,
RA   Boehm C., Briginshaw L., Caballero-Perez J., Catarino B., Chen F.,
RA   Chiyoda S., Chovatia M., Davies K., Delmans M., Demura T., Dierschke T.,
RA   Dolan L., Dorantes-Acosta A., Eklund D., Florent S., Flores-Sandoval E.,
RA   Fujiyama A., Fukuzawa H., Galik B., Grimanelli D., Grimwood J.,
RA   Grossniklaus U., Hamada T., Haseloff J., Hetherington A., Higo A.,
RA   Hirakawa Y., Hundley H., Ikeda Y., Inoue K., Inoue S., Ishida S., Jia Q.,
RA   Kakita M., Kanazawa T., Kawai Y., Kawashima T., Kennedy M., Kinose K.,
RA   Kinoshita T., Kohara Y., Koide E., Komatsu K., Kopischke S., Kubo M.,
RA   Kyozuka J., Lagercrantz U., Lin S., Lindquist E., Lipzen A., Lu C.,
RA   Luna E., Martienssen R., Minamino N., Mizutani M., Mizutani M.,
RA   Mochizuki N., Monte I., Mosher R., Nagasaki H., Nakagami H., Naramoto S.,
RA   Nishitani K., Ohtani M., Okamoto T., Okumura M., Phillips J., Pollak B.,
RA   Reinders A., Roevekamp M., Sano R., Sawa S., Schmid M., Shirakawa M.,
RA   Solano R., Spunde A., Suetsugu N., Sugano S., Sugiyama A., Sun R.,
RA   Suzuki Y., Takenaka M., Takezawa D., Tomogane H., Tsuzuki M., Ueda T.,
RA   Umeda M., Ward J., Watanabe Y., Yazaki K., Yokoyama R., Yoshitake Y.,
RA   Yotsui I., Zachgo S., Schmutz J.;
RT   "WGS assembly of Brassica rapa FPsc.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
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DR   EMBL; CM010628; RID79791.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A398AQ37; -.
DR   Proteomes; UP000264353; Chromosome a1.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.20; -; 2.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 2.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 3.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR000291; D-Ala_lig_Van_CS.
DR   InterPro; IPR011095; Dala_Dala_lig_C.
DR   InterPro; IPR011127; Dala_Dala_lig_N.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   PANTHER; PTHR23132:SF29; ATP-GRASP DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR   Pfam; PF07478; Dala_Dala_lig_C; 2.
DR   Pfam; PF01820; Dala_Dala_lig_N; 2.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00843; DALA_DALA_LIGASE_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT   DOMAIN          213..453
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          676..945
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   949 AA;  104622 MW;  6DA2947EE531357A CRC64;
     MSSTAIGVSL SVSSRIRRGG GGELDVERVL VTASPTTLKL NQTRRVVAGR FLRMKKRFHG
     TVAITKAEVD DGEEKRTSRN MRVGLICGGP SAERGISLNS VRSVLDHIQG NGISVSCYYI
     DPNLNAYAIS SAQVYSNTPA DFDFKLESLA QAFASLSELA EHLVSAVDIV FPVIHGRFGE
     DGGIQELLES HNIPFVGTGS VDCRRAFDKY EASLALKEHG FMSVPNYLVQ GTEVDESEIA
     QWFTDNQLDL EVGKVVVKPA NSGSSIGVKV AFGVKDSIKK ATELILEGID KRVVVEAFIE
     NAYEFTAIVL DVGSASDCHP VVLLPSEVEL KFHGSGDTKE NAIFDYRRKY LPTQQVTYHT
     PPRFPIHVIK SIREEASLLF KKLSLRDFAR FDGWYLTPTS NLASSASQTL TRSGDIIFTD
     INLISGMEQT SLFFQQASKV GFSHSNILRT IIYRASSRYP KLSWYNYDES SQGSTTMETP
     GDVQKVFVLF GGDTSERQVS VISGTNIWMN LQRFGDLKVT PCLLSSSLSN SMGPFPDKTE
     SDLDNREVWL LPYSVVLRHT VEEVLAACME AIDPDRARFT SLLQQQVKEE IMDALKNQSW
     FAGFDITDEV PMRFSLKDWV KLAKESEAIV FLSAHGGIGE DGTMQALLED EEVPYTGSGV
     HASRICMDKA MASKALSHLS EFGVQTISNE VKRTDDIIHE SIPAIWDELI TKFKCLTLCV
     KPARDGCSTG VARLCSSEDL AVYVQALRDC LPRIQANSFS KTHGMIEMPN PTPELLIFEP
     FIETDEVIVS SKSSEKLSWK GSRRWVEITV GVIGKHGSMR SLSPSLTVKE SGDILSLEEK
     FQGGTGINLT PPPTTIMSKE ALERCKRGIE LIAKTLGLEG FSRIDAFVHV ETGDGTNKDV
     MQVMAIEVNT VPGMTPSTVL IQQALAEQPP MYPPQFFRTL LNLAAQRVK
//
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