ID A0A1D8RXG5_9GAMM Unreviewed; 583 AA.
AC A0A1D8RXG5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Mur ligase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A3Q34_13305 {ECO:0000313|EMBL:AOW77740.1};
OS Colwellia sp. PAMC 20917.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=1816218 {ECO:0000313|EMBL:AOW77740.1, ECO:0000313|Proteomes:UP000177820};
RN [1] {ECO:0000313|EMBL:AOW77740.1, ECO:0000313|Proteomes:UP000177820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 20917 {ECO:0000313|EMBL:AOW77740.1,
RC ECO:0000313|Proteomes:UP000177820};
RA Kim H.-W.;
RT "Complete genome sequence of Colwellia sp. PAMC 20917.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP014944; AOW77740.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D8RXG5; -.
DR STRING; 1816218.A3Q34_13305; -.
DR KEGG; coz:A3Q34_13305; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000177820; Chromosome.
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 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 PANTHER; PTHR23135:SF18; CYANOPHYCIN SYNTHETASE; 1.
DR PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 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 Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Reference proteome {ECO:0000313|Proteomes:UP000177820}.
FT DOMAIN 189..405
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 430..500
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 583 AA; 63349 MW; 7C69D2435510D0DF CRC64;
MNNTITLTLD DQRRLTGKSL LWNKSGAIID AFVSGIDKQT VVDQWLIYVN QLLAAVDWQD
ESTCYRIFED GISLAISAPM DALYASCDVN EAAWDFACSK ILTGSISDTH QQEMDKTVTR
LKQMIAEEAN PALLNLIDLA IKNHVDYLVD DDEFSLGYGK SCQRWPVTSL PDPTQLNWQH
YQSIPIALVT GTNGKSTTVR IMSEIIKQSN KCCGVTSTDF IRVGEKIIDY GDYSGPGGAR
MLLRHPETET AILEVARGGI LRRGLPIDHV DAALITNIAE DHLGQYGINT VAGLAQTKAV
VAKALTSGVL VLNADDPYLT ALAPTLTVNK CWFSLNENNP VLQQHKAIGG AICFIRDGAI
FYCTEKTSTG ERLESMIVAV NDIPMTLNGA AQHNVQNALG ATALAKSLHI DSAVIGLALQ
NFSSNVDDNP GRGNQFKLNG ASVIMDFAHN VHGMNAMALT MANIPASRKF LMLSHAGDRS
NDDMIKMTKS ALKMKPDILV AAETVEYLRG RELGEISNLI AKVAIESGMS ADNIYFAEGP
YQGAQQIVNQ LSANDLALLI VLSERNKVIE LLTKKTNQTA GMS
//