ID K6YYH2_9ALTE Unreviewed; 563 AA.
AC K6YYH2;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Mur ligase family protein {ECO:0000313|EMBL:GAC16270.1};
GN ORFNames=GLIP_3659 {ECO:0000313|EMBL:GAC16270.1};
OS Aliiglaciecola lipolytica E3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Aliiglaciecola.
OX NCBI_TaxID=1127673 {ECO:0000313|EMBL:GAC16270.1, ECO:0000313|Proteomes:UP000006334};
RN [1] {ECO:0000313|EMBL:GAC16270.1, ECO:0000313|Proteomes:UP000006334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E3 {ECO:0000313|EMBL:GAC16270.1,
RC ECO:0000313|Proteomes:UP000006334};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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:GAC16270.1}.
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; BAEN01000068; GAC16270.1; -; Genomic_DNA.
DR RefSeq; WP_008846072.1; NZ_BAEN01000068.1.
DR AlphaFoldDB; K6YYH2; -.
DR STRING; 1127673.GLIP_3659; -.
DR eggNOG; COG0769; Bacteria.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000006334; 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: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, ECO:0000313|EMBL:GAC16270.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006334}.
FT DOMAIN 179..390
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 417..487
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 563 AA; 61904 MW; 98E9AC04B2F8EFDA CRC64;
MRLELDEVRR LTGPNLLWDK PGAILDVFID DVDPRSVVTV WQSWVDKLLQ TMQWPQSCTY
RLYSGGASMA LSAEMDALYT ACDVAEFAWE LSVAQMNGLP EVDWQLKAKQ LQVALSEEQN
PELLKILQQA EAHQVTAISD DDELSLGMGA SVRVWPIDQL PDLTELNWNA FRDIPRAFIT
GTNGKSTSVR LASEIAKAAG INAGVTSTDF IKVGEQIIDK GDYSGPGGAR MLLRDKRTEM
AFLEVARGGI LRRGIPVDNV NAALITNVAS DHLGQYGINT VEELAKVKFV VAKGLTPAGT
LVLNADNALV VEQAKELDCR ICWFSEDENH PLIKSNQQSA LPCVFVQNKQ FVYASGDTEK
QYIVDVADVP MTMKGAARHN IQNALGVIGL CMALKLPVDA IKRGLLNFGS SAKDNPGRGN
LYAFNGATVM LDFAHNAHSV AAMINTAKQL PANRYIVMFS NAGDRSDADI QQLTDEVRKL
DADHYIIAEL ERYLRGRQVY ELPKMVSAYL QRQGVEAALV ECVDSPLSGA KLALSLCRPG
DVLVLFCLDQ REEIHQLLIT NQD
//
