ID A0A0Q4MMF9_9GAMM Unreviewed; 482 AA.
AC A0A0Q4MMF9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASF13_07410 {ECO:0000313|EMBL:KQN56931.1};
OS Erwinia sp. Leaf53.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=1736225 {ECO:0000313|EMBL:KQN56931.1, ECO:0000313|Proteomes:UP000050856};
RN [1] {ECO:0000313|EMBL:KQN56931.1, ECO:0000313|Proteomes:UP000050856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN56931.1,
RC ECO:0000313|Proteomes:UP000050856};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN56931.1, ECO:0000313|Proteomes:UP000050856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN56931.1,
RC ECO:0000313|Proteomes:UP000050856};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQN56931.1}.
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DR EMBL; LMLK01000021; KQN56931.1; -; Genomic_DNA.
DR RefSeq; WP_056237064.1; NZ_LMLK01000021.1.
DR AlphaFoldDB; A0A0Q4MMF9; -.
DR STRING; 1736225.ASF13_07410; -.
DR Proteomes; UP000050856; Unassembled WGS sequence.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic 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 PANTHER; PTHR43024; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR PANTHER; PTHR43024:SF1; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE 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.
PE 4: Predicted;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Reference proteome {ECO:0000313|Proteomes:UP000050856}.
FT DOMAIN 132..316
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 349..410
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 482 AA; 51012 MW; 216A7D4BA631AECA CRC64;
MAAEAEKRVS PATQHLFADK DRIWTAEEVQ AATGGEWVTP PPPGWAASGL SIYAPACQPG
NMAVVRSEAD ESGMPARAAL RLVPPPACLI TTDPAPLLHS GLPLLKISEG FTAIINLGRY
ARDQIRGKVL GVTGSAGKTT CVAMLADALS AWGASSKSAH NANLPRGVAW NLASVPRDTP
HVILEMAIGR MGVSSRMARP DIAIFTNIQP AHLGENSTVR DVALTKSAIF FGMQPGGIAI
LNRDMLEWET VHQAATAKGL SVLHYGSHQS SDARLIAYDA LQQRVTAEVC GQPLSYSLAA
GGRHMALNSL AVLAAVSALG YPLEPALARL AGFTALAGRG EQKRVTLNGT GFELIDDAYN
ANPGSMQAAL EQLSERPCSG RRIAVLSEMK ELGPESEGYH SQLAAQLNDS SIDGICLVGA
IWQGCWAQLK PEKRIALLDD PQQLKPLLLA QLRPDDTVLF KGSNSTGLHQ IVSWIDGQPG
AL
//
