ID A0A1Q5PCP6_9BACT Unreviewed; 901 AA.
AC A0A1Q5PCP6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00047};
DE EC=6.3.2.4 {ECO:0000256|HAMAP-Rule:MF_00047};
DE AltName: Full=D-Ala-D-Ala ligase {ECO:0000256|HAMAP-Rule:MF_00047};
DE AltName: Full=D-alanylalanine synthetase {ECO:0000256|HAMAP-Rule:MF_00047};
GN Name=ddl {ECO:0000256|HAMAP-Rule:MF_00047};
GN ORFNames=A3841_16490 {ECO:0000313|EMBL:OKL39963.1};
OS Pontibacter flavimaris.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=1797110 {ECO:0000313|EMBL:OKL39963.1, ECO:0000313|Proteomes:UP000186551};
RN [1] {ECO:0000313|EMBL:OKL39963.1, ECO:0000313|Proteomes:UP000186551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S10-8 {ECO:0000313|EMBL:OKL39963.1,
RC ECO:0000313|Proteomes:UP000186551};
RA Zhang G., Zhang R.;
RT "Genome sequence of Pontibacter sp. nov., of the family cytophagaceae,
RT isolated from marine sediment of the Yellow Sea, China.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00047}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) +
CC phosphate; Xref=Rhea:RHEA:11224, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57416,
CC ChEBI:CHEBI:57822, ChEBI:CHEBI:456216; EC=6.3.2.4;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00047};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00047}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047}.
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871, ECO:0000256|HAMAP-Rule:MF_00047}.
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:OKL39963.1}.
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DR EMBL; LVWA01000005; OKL39963.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5PCP6; -.
DR STRING; 1797110.A3841_16490; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000186551; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-UniRule.
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-UniRule.
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; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 3.
DR HAMAP; MF_00047; Dala_Dala_lig; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR000291; D-Ala_lig_Van_CS.
DR InterPro; IPR005905; D_ala_D_ala.
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; 4.
DR Pfam; PF01820; Dala_Dala_lig_N; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 3.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00843; DALA_DALA_LIGASE_1; 1.
DR PROSITE; PS00844; DALA_DALA_LIGASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_00047};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_00047};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00047};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00047};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW Rule:MF_00047}.
FT DOMAIN 158..440
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 640..889
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 901 AA; 101896 MW; 6C329B5D55DAC7CB CRC64;
MMKVGIIFGG PSREREISFA GGRTVYDNLD KSLFEAVPVF VDSLGNFILL DWQYIYKGTI
RDFYPPVEAL PESEHGLQIY LESLGELSIA EQDKIIAKAG KRLQPNEFKN HFDFAFLALH
GPYGEDGSIQ GLLEWYHIPY SGSGILPSAI GIDKAAQKEM LKQHGFPTPD YRTIQYNDWS
NKENRRQVFE QLKAALNLPL VLKAPHQGSS IGVSIIKEDD FAAFEAGMER SFFTKTIYKS
QWLAMGEEKQ LVSMKQLVDI REGIGMPVVL EDGQIIYHPE ELFNHINHTF NTTATDSITL
TNVEHEQQVL VEAFIQGREF SCIVVQDEQG QPIALPPTEI VKGSEVFDYR SKYLPGLSRK
ITPINLPTEQ IQSIRQATSR LFRAFGFNVY ARLDGFITEA GDIFLNDPNT TSGMLPSSFF
FHQAAEIGLN PSQFLTYIIR TSVSERLKTG KDTVKLSRLL QQLDKSIKDE QVHRQEKIRV
GVIMGGYSSE RHISVESGRN IYEKLSSSVK YEPLPIFLTG SNESHRLYAI PINIMLKDNA
DDIKEKVLYF EQGGKPHPVL AQIIEEASSI TKKYTGRSLQ EPQRITYDQL KNLVDVVFIA
LHGRPGEDGA LQQELEKLHI PYNGSGIRSS QITINKYETN EILARHGVSV AHHKMAMKED
WLQDKETFYQ SLEAEFKYPF IAKPADDGCS SAVKKIKNRQ ELDAFSTLIF REMEELDTEC
ARTLSLGFKE EFPNKAGFLV ETLISRNGAK HFLEITGGLL TKYNPDGTVN YEVFEASEAL
AEGEVLSLEE KFLAGEGQNI TPARYAADPE RRQKISDQVK EDLRRVAQIL NIEGYARIDA
FVRVLENNEV ETIIIEVNSL PGMTPATCIF HQTAINGYKP YDFIDRILSY GIERTRMKAN
I
//
