ID A0A095SUK2_9FLAO Unreviewed; 451 AA.
AC A0A095SUK2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Peptidoglycan synthetase {ECO:0000313|EMBL:KGD68049.1};
GN ORFNames=LG45_07060 {ECO:0000313|EMBL:KGD68049.1};
OS Flavobacterium aquatile LMG 4008 = ATCC 11947.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1453498 {ECO:0000313|EMBL:KGD68049.1, ECO:0000313|Proteomes:UP000029554};
RN [1] {ECO:0000313|EMBL:KGD68049.1, ECO:0000313|Proteomes:UP000029554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 4008 {ECO:0000313|EMBL:KGD68049.1,
RC ECO:0000313|Proteomes:UP000029554};
RA Gale A.N., Pipes S.E., Newman J.D.;
RT "Whole Genome Shotgun of Flavobacterium aquatile LMG 4008.";
RL Submitted (SEP-2014) 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:KGD68049.1}.
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DR EMBL; JRHH01000003; KGD68049.1; -; Genomic_DNA.
DR RefSeq; WP_035125633.1; NZ_MUGQ01000004.1.
DR AlphaFoldDB; A0A095SUK2; -.
DR STRING; 1453498.LG45_07060; -.
DR eggNOG; COG0773; Bacteria.
DR OrthoDB; 9804126at2; -.
DR Proteomes; UP000029554; Unassembled WGS sequence.
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; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000029554}.
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"
FT DOMAIN 306..382
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 451 AA; 50716 MW; 9A27F6C91C0E0DF2 CRC64;
MRTHFIAIGG AAMHNLAIAL HNKGYQVTGS DDAIFEPSKS RLEKKGLLPI EMGWFPEKIT
SDIEAIILGM HAKADNPELL KAEELGLKIY SYPEFLYEQS KNKTRVVIGG SHGKTTITSM
ILHVMHYHNI EVDYMVGAQL EGFDTMVHLT ETNDFIVLEG DEYLSSPIDR RPKFHLYQPN
IALLSGIAWD HINVFPTFEN YVEQFEIFVN QITKGGILVY NEEDETVKKV AEETTNTIRR
LPYATPNYSV EDGTTLLETP EGPMPIEVFG AHNLNNLAGA KWICQNMGVD EADFYEAIAS
FKGASKRLEK IAEGKGKVAY KDFAHSPSKV SATTKAVKNQ YPNRTLIACL ELHTYSSLNA
EFLKEYQNAL DAADVAVVFY SPDAVKIKQL EEVTYDQIAQ SFQREDLIIY TNPADFKNFL
FSQNFDNSAL LLMSSGNYGG LNFDEVKELM R
//