ID Q6IVP7_9GAMM Unreviewed; 432 AA.
AC Q6IVP7;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Predicted UDP-N-acetylmuramate: L-alanyl-diaminopimelate ligase {ECO:0000313|EMBL:AAT38601.1};
GN ORFNames=eBACHOT4E07.40 {ECO:0000313|EMBL:AAT38601.1};
OS uncultured gamma proteobacterium eBACHOT4E07.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; SAR86 cluster;
OC environmental samples.
OX NCBI_TaxID=279908 {ECO:0000313|EMBL:AAT38601.1};
RN [1] {ECO:0000313|EMBL:AAT38601.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15305915; DOI=10.1111/j.1462-2920.2004.00676.x;
RA Sabehi G., Beja O., Suzuki M.T., Preston C.M., DeLong E.F.;
RT "Different SAR86 subgroups harbour divergent proteorhodopsins.";
RL Environ. Microbiol. 6:903-910(2004).
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DR EMBL; AY619685; AAT38601.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6IVP7; -.
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; IPR005757; Mpl.
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 NCBIfam; TIGR01081; mpl; 1.
DR PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 1.
DR PANTHER; PTHR43445:SF5; UDP-N-ACETYLMURAMATE--L-ALANYL-GAMMA-D-GLUTAMYL-MESO-2,6-DIAMINOHEPTANDIOATE LIGASE; 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:AAT38601.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT DOMAIN 2..98
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 106..283
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 303..349
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 432 AA; 48812 MW; 08967B25E41A00DE CRC64;
MRIHILGICG TFMAGLAQIL KESGHDVSGA DAKFYPPMSD YLKKIGIKTI EGYEKKSLPE
ADLYVIGNAL SRGNECVEEI LDQKLPYVSG PEMLGKELKN RNVFAISGTH GKTTTSYMLA
HIFLDQGREI GYLVGGISDD FDNSACLGKD PIFVIEADEY DSAFFDKRSK FIHYSPTNLI
INNIEFDHAD IFNDIEDVKK QFHHLIKIIK SSGNIIYFDD DSTSKEVIEK GIWCSKIGIN
SNGVKADFES KELIIDDEIF QLNELPLIGE HNFKNYVCSI LAAKLEGISE TESINSLKKF
KGVKRRMDFI KEISGIRIYD DFAHHPTAIK LSCSAIRNKY SDKKILGLIE LGSNTMSSGY
HKENLINSFG SLDEFLMLDP NKNYKINNAF DSENELLKNL EEKIFDYDII LIMTNKDSQK
FINPIINSIE KK
//
