ID A0A1I2F0P9_9BACT Unreviewed; 552 AA.
AC A0A1I2F0P9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=D-alanine-D-alanine ligase {ECO:0000313|EMBL:SFE98735.1};
GN ORFNames=SAMN05216167_1248 {ECO:0000313|EMBL:SFE98735.1};
OS Spirosoma endophyticum.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX NCBI_TaxID=662367 {ECO:0000313|EMBL:SFE98735.1, ECO:0000313|Proteomes:UP000198598};
RN [1] {ECO:0000313|EMBL:SFE98735.1, ECO:0000313|Proteomes:UP000198598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26130 {ECO:0000313|EMBL:SFE98735.1,
RC ECO:0000313|Proteomes:UP000198598};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOLQ01000024; SFE98735.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2F0P9; -.
DR STRING; 662367.SAMN05216167_1248; -.
DR OrthoDB; 9813261at2; -.
DR Proteomes; UP000198598; 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 GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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; 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; D-ALANINE--D-ALANINE LIGASE; 1.
DR PANTHER; PTHR23132:SF0; D-ALANINE-D-ALANINE LIGASE FAMILY; 1.
DR Pfam; PF07478; Dala_Dala_lig_C; 2.
DR Pfam; PF01820; Dala_Dala_lig_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:SFE98735.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000198598}.
FT DOMAIN 228..431
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 552 AA; 61291 MW; F25EA0E3A34FCDDE CRC64;
MKIGIFFGGP AREREVSFAG GRTALANLDK GLFEPILIFV DGRGRFRLAT SDFLQSASLR
EALPQDDSGF SVYDESLSAD VLDPLLPELR PEQFRDHFDL AFLAMHGPDC EDGAIQGLLE
WHKMPYTGPG LVGSAVGINK ILQNELIALA NGQQKKTATI NRDAYEQADK AQFFQSLIEH
LGLPIVVKAP HQGSSIGVAI VREADLTQFC RSVQQCFFTM SIQPDGWSKL SEWADLSADD
KRELAQNMVS LDAGISFPVV IEQTGDVIKH PKEFIDKLDA LTRDQSVGAI TLASLNAEDE
VLFEEFIRGQ EFSCGVIQDD DQIAIALPPT EIYNVTSFDF ESKYKLNTTK KRIPVETSLE
NNRKIQLAVA HVFTRLGINV YSRIDGFLTP AGDVLLHDPN TIPGMSPSSL IFKQMAEIGL
NLANSLTYLI RQSLRERIRT GKDTFHLKHL LADLDAQLAN RKMSPLPERV VSFGDSDEGF
AAAKQKYNEL AASGTVRPSL MYIKSKQEAY EIPVNLLFKD TIAELETALS QPRHPLLVET
AEHARHITER YV
//
