ID A0A2K1E514_9FLAO Unreviewed; 451 AA.
AC A0A2K1E514;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Peptidoglycan synthetase {ECO:0000313|EMBL:PNQ75360.1};
GN ORFNames=C1T31_04310 {ECO:0000313|EMBL:PNQ75360.1};
OS Hanstruepera neustonica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Hanstruepera.
OX NCBI_TaxID=1445657 {ECO:0000313|EMBL:PNQ75360.1, ECO:0000313|Proteomes:UP000236641};
RN [1] {ECO:0000313|EMBL:PNQ75360.1, ECO:0000313|Proteomes:UP000236641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM19743 {ECO:0000313|EMBL:PNQ75360.1,
RC ECO:0000313|Proteomes:UP000236641};
RA He R.-H., Du Z.-J.;
RT "The draft genome of Hanstruepera neustonica JCM19743.";
RL Submitted (JAN-2018) 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:PNQ75360.1}.
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DR EMBL; POWF01000001; PNQ75360.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1E514; -.
DR OrthoDB; 9804126at2; -.
DR Proteomes; UP000236641; 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: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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000236641}.
FT DOMAIN 3..101
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; 50528 MW; 99B701C068934500 CRC64;
MNVHFIAIGG AAMHNLAIAL HNKGYHVTGS DDTIFDPSKS RLEAKGLLPE QFGWFPEKIN
NSLDAIVLGM HAKADNPELL KAQELGLKIY SYPEFLYEQS KDKTRVVIGG SHGKTTITSM
ILHVMHYHDR DVDYMVGAQL EGFDVMVKLT EDNDFMVLEG DEYLSSPIDK RPKFHLYKPN
IALLSGIAWD HINVFPTYEN YVEQFSIFVD SIVRGGSITY NAEDPEVARV VEASENTIRK
LPYYTPEYTV ENGETLLETP EGPLPIGVFG KHNLNNLAGA KWICQHMGID EDDFYEAIAT
FKGASKRLEK IAESKTSVAY KDFAHSPSKV AATTKALKEQ FPNRTLVACL ELHTYSSLNA
EFLKEYKGAL DAADVAVVFY SPHAVEIKKL EEVTHQQIAD AFERDDLIIY TNPDDFKNYL
FSQDFNNKAL LLMSSGNYGG LDFDEVKGLI G
//