ID A0A1S2HIW3_9MICO Unreviewed; 548 AA.
AC A0A1S2HIW3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208};
DE EC=6.3.2.- {ECO:0000256|HAMAP-Rule:MF_00208};
DE AltName: Full=UDP-MurNAc-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208};
GN Name=murE {ECO:0000256|HAMAP-Rule:MF_00208};
GN ORFNames=BIU96_17465 {ECO:0000313|EMBL:OII11182.1};
OS Curtobacterium sp. MCBA15_008.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1898736 {ECO:0000313|EMBL:OII11182.1, ECO:0000313|Proteomes:UP000180168};
RN [1] {ECO:0000313|EMBL:OII11182.1, ECO:0000313|Proteomes:UP000180168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCBA15_008 {ECO:0000313|EMBL:OII11182.1,
RC ECO:0000313|Proteomes:UP000180168};
RA Chase A.B., Arevalo P., Polz M.F., Berlemont R., Martiny J.B.;
RT "Evidence for ecological flexibility in the cosmopolitan genus
RT Curtobacterium.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the addition of an amino acid to the nucleotide
CC precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the
CC biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000256|HAMAP-
CC Rule:MF_00208}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00208};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00208}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208}.
CC -!- PTM: Carboxylation is probably crucial for Mg(2+) binding and,
CC consequently, for the gamma-phosphate positioning of ATP.
CC {ECO:0000256|HAMAP-Rule:MF_00208}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
CC {ECO:0000256|ARBA:ARBA00005898, ECO:0000256|HAMAP-Rule:MF_00208}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00208}.
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:OII11182.1}.
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DR EMBL; MJGN01000025; OII11182.1; -; Genomic_DNA.
DR RefSeq; WP_071292868.1; NZ_MJGN01000025.1.
DR AlphaFoldDB; A0A1S2HIW3; -.
DR STRING; 1898736.BIU96_17465; -.
DR OrthoDB; 9800958at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000180168; 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
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-UniRule.
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; 3.40.1390.10; MurE/MurF, N-terminal domain; 1.
DR HAMAP; MF_00208; MurE; 1.
DR InterPro; IPR018109; Folylpolyglutamate_synth_CS.
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 InterPro; IPR035911; MurE/MurF_N.
DR InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
DR PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 1.
DR PANTHER; PTHR23135:SF4; UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC; 1.
DR Pfam; PF01225; Mur_ligase; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR SUPFAM; SSF63418; MurE/MurF N-terminal domain; 1.
DR PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00208};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_00208};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_00208};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_00208};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_00208};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00208};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00208};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00208};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW Rule:MF_00208}.
FT DOMAIN 40..110
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 131..332
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 378..461
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT REGION 521..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT BINDING 133..139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT BINDING 175..176
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT BINDING 202
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT BINDING 210
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
FT MOD_RES 242
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208"
SQ SEQUENCE 548 AA; 59246 MW; E4E188AF2934B24F CRC64;
MSARIPPVLR PEHPTPRAVA ELANAFGLRV VGSLDAVETT GVTLSAAEVQ PGDLFVGVHG
ANRHGAQFAT EAAERGAVAV LTDADGVALA EPSGLPVLVV DDPRAALGDV SAWVYRTHPD
EATDLPQLFA VTGTNGKTST SYILEGILKQ LGLVTGLSST AERHIGTLSV TSRLTTPEAS
EMHALLARMR ESEVRAVAVE VSAQALSRHR VDGIVFDVAA FTNLSHDHLD DYADMEEYYR
AKLPLFEPEH ARRGVVSLDT DWGHRVVQDS RIPVTTITVH PDVEAEWHVD IVEAHAAYTE
FRLTGPEDRE LTTRVPLIGW HMAANAALAI VMLVEGGFEL GTIAHALESN HRHYADEDGD
RGDHGQQRTV SAIECYLPGR TERVSGDRGP SVYVDFGHSP DAFENTLAAV RQFTPGKVLM
LFGADGDRDK TKRADMARIA AAGSDILVVT DHHPRFEDAA SIRKTLVDAA RAAYPEHEIH
EVSPPEAAIR TAVGLLSEGD SILWAGPGHQ DYRDIQGVRT PYSARDEARQ ALREAGWEPN
SGPAEDVR
//
