ID A0A0N7HZE8_9CAUL Unreviewed; 466 AA.
AC A0A0N7HZE8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=UDP-N-acetylmuramate--alanine ligase {ECO:0000313|EMBL:ALJ07868.1};
GN ORFNames=JL11_05565 {ECO:0000313|EMBL:ALJ07868.1};
OS Brevundimonas sp. DS20.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=1532555 {ECO:0000313|EMBL:ALJ07868.1, ECO:0000313|Proteomes:UP000059212};
RN [1] {ECO:0000313|EMBL:ALJ07868.1, ECO:0000313|Proteomes:UP000059212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS20 {ECO:0000313|EMBL:ALJ07868.1,
RC ECO:0000313|Proteomes:UP000059212};
RA Scott D., Ely B.;
RT "Conservation of the essential genome among Caulobacter and Brevundimonas
RT species.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP012897; ALJ07868.1; -; Genomic_DNA.
DR RefSeq; WP_054764784.1; NZ_CP012897.1.
DR AlphaFoldDB; A0A0N7HZE8; -.
DR STRING; 1532555.JL11_05565; -.
DR KEGG; brd:JL11_05565; -.
DR Proteomes; UP000059212; Chromosome.
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:ALJ07868.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT DOMAIN 9..107
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 115..294
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 315..361
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 466 AA; 49492 MW; 3924C62D8486751D CRC64;
MNQDASYFFC GIGGSGMLPL ALIVQAQGAR IEGSDRALDQ GRTPEKFDWL RAHGVTLHPQ
DGSGVTRPDQ IVVATGAVEE TVPDIGAARR VGAAIKTRPE LLSELFNAAP TSIGVAGTSG
KSTITGMIAW ILHQTGRDPT VMNGAVMKNF ADADHPFASA LIGGSDLFVS EVDESDGSIA
RYVPTVAVVS NISLDHKSME ELRDLFGGFV QRAATAVLNL DNPETAALAQ ELTPGKAITF
ALGEEAADLS AHDLQPQPTG MRFRLIEGWS EFDVRLNVPG AHNVANALAA LGAVKALGVS
TAEAVKALES FAGIRRRMEV VGTVDAVTVI DDFAHNPDKI AATLKTLHAF DGRLLILFQP
HGFGPLKLMR REFIDGFVGL MREDDVLLMP EPVYYGGTTD RSVGSEAVAE GVREAGRQAE
ALPDRAACGD RIVEMARPGD RILVMGARDD TLSSFAADLL ERLGAR
//
