ID A0A2Z4GAR4_9BACT Unreviewed; 481 AA.
AC A0A2Z4GAR4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Peptidoglycan synthetase {ECO:0000313|EMBL:AWV98297.1};
GN ORFNames=DJ013_08990 {ECO:0000313|EMBL:AWV98297.1};
OS Arcticibacterium luteifluviistationis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Arcticibacterium.
OX NCBI_TaxID=1784714 {ECO:0000313|EMBL:AWV98297.1, ECO:0000313|Proteomes:UP000249873};
RN [1] {ECO:0000313|EMBL:AWV98297.1, ECO:0000313|Proteomes:UP000249873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM1504 {ECO:0000313|EMBL:AWV98297.1,
RC ECO:0000313|Proteomes:UP000249873};
RA Li Y., Qin Q.-L.;
RT "Complete genome sequence of Arcticibacterium luteifluviistationis SM1504T,
RT a cytophagaceae bacterium isolated from Arctic surface seawater.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP029480; AWV98297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z4GAR4; -.
DR KEGG; als:DJ013_08990; -.
DR OrthoDB; 9804126at2; -.
DR Proteomes; UP000249873; Chromosome.
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:UP000249873}.
FT DOMAIN 7..101
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 113..285
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 311..386
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 481 AA; 54240 MW; C0F2B0DFA637884D CRC64;
MSKTIKNIHF IAVGGAIMHN LALALLQKGY RVTGSDDEIY DPAKSRLEKA GILPKKIGWN
TDNITEDLDA VILGMHARKD NPELKKAEEL GLKVYSFPEY VFEQTKNKQR IAIAGSHGKT
SITSIILHVL KYYNRNFDYL VGAQIEGFDL MVKLTDDAPV IILEADEYLS SALEMKSKFL
FYHPHITLIS GIAWDHFNVF PKFEDYVKAF EQLADGMPKA STLLWDETDD IANIIGKQVR
DEVNQIPYKA HPYEVKDGKI SLKTKNGPVP LKIFGEHNMK NLQGAKEILE KIAITEDMFY
KAIQSFSGAA KRLEKLGESK NTVIYRDFAH APSKVGATTN AGKELYPDRK LVACYELHTY
SSLSKDFLPH YAEKLNAADD AVVFYSPHTV EMKKMPPISP EEIKAAFGRE DLKIFTTAEE
LQDYLTSINW YKANLLLMSS GTFGGTDLPK LSETILKLPV KKEARSTQKK KSWKGIFKKK
S
//
