ID A0A1D7QY55_9BACI Unreviewed; 714 AA.
AC A0A1D7QY55;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 05-FEB-2025, entry version 42.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=BBEV_2606 {ECO:0000313|EMBL:AOM83945.1};
OS Salisediminibacterium beveridgei.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Salisediminibacterium.
OX NCBI_TaxID=632773 {ECO:0000313|EMBL:AOM83945.1, ECO:0000313|Proteomes:UP000094463};
RN [1] {ECO:0000313|EMBL:AOM83945.1, ECO:0000313|Proteomes:UP000094463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MLTeJB {ECO:0000313|EMBL:AOM83945.1,
RC ECO:0000313|Proteomes:UP000094463};
RA Hanson T.E., Mesa C., Basesman S.M., Oremland R.S.;
RT "The complete genome sequence of Bacillus beveridgei MLTeJB.";
RL Submitted (AUG-2015) 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; CP012502; AOM83945.1; -; Genomic_DNA.
DR RefSeq; WP_069365870.1; NZ_CP012502.1.
DR AlphaFoldDB; A0A1D7QY55; -.
DR STRING; 632773.BBEV_2606; -.
DR KEGG; bbev:BBEV_2606; -.
DR PATRIC; fig|632773.3.peg.2739; -.
DR OrthoDB; 9813261at2; -.
DR Proteomes; UP000094463; Chromosome.
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:0016787; F:hydrolase 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 Gene3D; 3.30.70.360; -; 1.
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 Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR011095; Dala_Dala_lig_C.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR PANTHER; PTHR23132:SF23; D-ALANINE--D-ALANINE LIGASE B; 1.
DR Pfam; PF07478; Dala_Dala_lig_C; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000094463}.
FT DOMAIN 119..320
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 714 AA; 79855 MW; A73D65D278C8F127 CRC64;
MKIAIVYNRE SQAVINLFGT PNREKYGLET IKKIKDGLQT LGHQVKTFEG DKNIIQKLEE
YMPSVISGER PGLVFNLSYG IQGKGRYMHV PGILEMIGVP YVGSGPETHA MALDKVVTKM
ILLQKGLPTP RFAELEKPDS PITAELTYPL IVKPKNEAVS FGLKIVHNEE ELREGVKIIY
DNFHSPTLVE EYIEGREVNV GLLGNSPVQA LPAVELTFGE GPQIYTYEDK TSGQGSRVQK
VCPAPLGDEL TAKVQKLAID TFHALNCFDT ARVDFRIDKD GNPYILEVNS MASLGADGSF
VYAAQTLGMS YAEIMNRIVE VTSERYFGPQ FVVSADESGE KKGMDLFEVI TKNRSGLEKD
LKMWTNMSSR TEDPVGLSSV RKKIEERAAK LGLQLNKQYT NGRSAWTWET KKGFKDGTLL
VVPIDVPGDR TGYPVPYRTE QEWIYGEGVA SSRGGLTTMF HALTALKDTK KLSPRKIGVF
FYADEGRGMR YSTAAFEQAV EHAGEVIVLQ PGFMEGKIVD QRRGFKQFNV IVEGDPVRMG
KSTRDPDVLT YFIKRADELQ SLSNRRKKLA VAMQDVKSER YSVLMPHRVV ATFSITYIDP
ELARQAEKQL RETFNSNGTS IRTYVEEIVD RKPMSRKKNH PLRDRLHELS ESWNIPYGTE
SSLLPSAAGI VPKDIPAICG FAPASKDLFT PNEALHRREL AQRTLLLALH LEGE
//
