ID A0A0H0XNS4_9SPHN Unreviewed; 471 AA.
AC A0A0H0XNS4;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=UDP-N-acetylmuramate--alanine ligase {ECO:0000313|EMBL:KLI63676.1};
GN ORFNames=AAV99_08045 {ECO:0000313|EMBL:KLI63676.1};
OS Aurantiacibacter marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=874156 {ECO:0000313|EMBL:KLI63676.1, ECO:0000313|Proteomes:UP000053455};
RN [1] {ECO:0000313|EMBL:KLI63676.1, ECO:0000313|Proteomes:UP000053455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HWDM-33 {ECO:0000313|EMBL:KLI63676.1,
RC ECO:0000313|Proteomes:UP000053455};
RA Zhuang L., Liu Y., Shao Z.;
RT "The draft genome sequence of Erythrobacter marinus HWDM-33.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KLI63676.1}.
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DR EMBL; LBHU01000002; KLI63676.1; -; Genomic_DNA.
DR RefSeq; WP_047093490.1; NZ_LDCP01000002.1.
DR AlphaFoldDB; A0A0H0XNS4; -.
DR STRING; 874156.GCA_001021555_01710; -.
DR PATRIC; fig|874156.12.peg.1654; -.
DR OrthoDB; 9804126at2; -.
DR Proteomes; UP000053455; Unassembled WGS sequence.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR004101; Mur_ligase_C.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR InterPro; IPR000713; Mur_ligase_N.
DR PANTHER; PTHR43445:SF3; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE; 1.
DR PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 1.
DR Pfam; PF01225; Mur_ligase; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF51984; MurCD N-terminal domain; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KLI63676.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000053455}.
FT DOMAIN 14..112
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 120..301
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 322..389
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 471 AA; 49786 MW; 63BE7D48B684423C CRC64;
MNDTTNISAR SYFFCGIGGS GMLPLGQIVK GMGAEVGGSD RSFDQGRTPE KFAALERQGY
ALFPQDGSGL TSGDQVLIAS AAIEDTVPEI ARAKELGCER LTRAELLARL FNDAPQSIAI
GGTSGKSTTT AMLGWIMQAT GRAPTIMNGA VMKNFVSEER PFASAVVGDG ETFVSEVDES
DGSIALYRPS VALLLNVSLD HKSMNELREL FGNFLLVADR GVVNADDLEA FRLVAQANEP
LTFGIDNSCA ALGIAEGSIA DGPTKQAALV VDRRDDSEHA LRLAMPGRHN LSNALAAIAA
ANAAGVPVAE AVAALADFKG LARRFDIVGT SANGVTVIDD FGHNPEKARA TLRTLKAHEG
RVIAFFQPHG YGPLRQMGAE LAETFAEELG PDDLTILCDP VYFGGTVDRS EGSERIIDLI
AKAGGKALHI NTREGCGDFI VQNARPGDRI AVMGARDDTL TEFAESLLQR L
//
