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Database: UniProt
Entry: A0A2K1E514_9FLAO
LinkDB: A0A2K1E514_9FLAO
Original site: A0A2K1E514_9FLAO 
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
//
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