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Database: UniProt
Entry: A4BTL3_9GAMM
LinkDB: A4BTL3_9GAMM
Original site: A4BTL3_9GAMM 
ID   A4BTL3_9GAMM            Unreviewed;       348 AA.
AC   A4BTL3;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN   ORFNames=NB231_00250 {ECO:0000313|EMBL:EAR20969.1};
OS   Nitrococcus mobilis Nb-231.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Nitrococcus.
OX   NCBI_TaxID=314278 {ECO:0000313|EMBL:EAR20969.1, ECO:0000313|Proteomes:UP000003374};
RN   [1] {ECO:0000313|EMBL:EAR20969.1, ECO:0000313|Proteomes:UP000003374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nb-231 {ECO:0000313|EMBL:EAR20969.1,
RC   ECO:0000313|Proteomes:UP000003374};
RA   Waterbury J., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA   Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAR20969.1}.
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DR   EMBL; AAOF01000014; EAR20969.1; -; Genomic_DNA.
DR   RefSeq; WP_004998606.1; NZ_CH672427.1.
DR   AlphaFoldDB; A4BTL3; -.
DR   STRING; 314278.NB231_00250; -.
DR   eggNOG; COG1181; Bacteria.
DR   HOGENOM; CLU_039268_2_0_6; -.
DR   OrthoDB; 9800957at2; -.
DR   Proteomes; UP000003374; Unassembled WGS sequence.
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   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR011095; Dala_Dala_lig_C.
DR   PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR   PANTHER; PTHR23132:SF0; D-ALANINE-D-ALANINE LIGASE FAMILY; 1.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003374}.
FT   DOMAIN          122..335
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   348 AA;  38520 MW;  35BABE486FE692E1 CRC64;
     MSARISTRSI DVAVLLGDPR LPYAYAIGAC FGAEEQNAVE QLKTALAALE GFTFTYLDDH
     TTLLDDLRQR PPSLAFNLCD VGFRNDTARE LNIPALLEIL NISYSGADPV GMSLATDKSI
     VRVVARSLGI PVPNEMFVDL GADPLVLPAL YPALIKPNFS DGSFGITADC VAHDAAEAER
     YLHWLAGELE RPEALIQDFL TGTEYTVGLI GNASQGFTYL PPLEVDYSRL DPELPPILSY
     ASKADPDSPY WQKLRFRRAR IDEVTRGRLY EYCTLLFKRL GLRDYGRFDF RAGADGEPRL
     LEVNHNPAWA WDGKLSLMAS YAGYSYSDLL RLILAAAMRR VDLGVAQD
//
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