ID A0A0Q7FMC1_9FLAO Unreviewed; 451 AA.
AC A0A0Q7FMC1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Peptidoglycan synthetase {ECO:0000313|EMBL:KQW97607.1};
GN ORFNames=ASC72_14505 {ECO:0000313|EMBL:KQW97607.1};
OS Flavobacterium sp. Root420.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1736533 {ECO:0000313|EMBL:KQW97607.1, ECO:0000313|Proteomes:UP000051729};
RN [1] {ECO:0000313|EMBL:KQW97607.1, ECO:0000313|Proteomes:UP000051729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root420 {ECO:0000313|EMBL:KQW97607.1,
RC ECO:0000313|Proteomes:UP000051729};
RX PubMed=26633631; DOI=.1038/nature16192;
RA Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E., Rott M.,
RA Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M., Huttel B.,
RA McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL Nature 528:364-369(2015).
RN [2] {ECO:0000313|Proteomes:UP000051729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root420 {ECO:0000313|Proteomes:UP000051729};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000051729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root420 {ECO:0000313|Proteomes:UP000051729};
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:KQW97607.1}.
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DR EMBL; LMEF01000032; KQW97607.1; -; Genomic_DNA.
DR RefSeq; WP_056195231.1; NZ_LMEF01000032.1.
DR AlphaFoldDB; A0A0Q7FMC1; -.
DR STRING; 1736533.ASC72_14505; -.
DR OrthoDB; 9804126at2; -.
DR Proteomes; UP000051729; 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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036565; Mur-like_cat_sf.
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; 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;
FT DOMAIN 3..102
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 108..280
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
SQ SEQUENCE 451 AA; 50607 MW; 5E5331B683A249F9 CRC64;
MKTHFIAIGG SAMHNLALAL HNKGYQVTGS DDAIFEPSKS RLEKKGILPA ELGWFPEKIT
ADIEAVILGM HAKADNPELL KAQELGLKIY SYPEFLYEQS KNKTRVVIGG SHGKTTITSM
ILHVMHYHNI EVDYMVGAQL EGFDTMVHLT EENDFMVLEG DEYLSSPIDR RPKFHLYQPN
IALISGIAWD HINVFPTYEN YVEQFEIFIQ KITNGGILVY NENDPEVKRV AEAATNPIRK
LSYHTPEYTV SDGVTLLKTP EGDMPIEVFG AHNLNNLAGA KWICQNMGVD EADFYEAIAS
FKGASKRLEK IAEGKGKVAY KDFAHSPSKV AATTKAVKEQ YPNRTLVACL ELHTYSSLNA
EFLKEYEGAL EYADVAVVFY SPDAVKIKQL EEVTYEQIAN SFNREDLIIY TNPSEFKEYL
FNLNLENSAL LLMSSGNYGG LNFDEVKSLI N
//
