ID F2I0M4_PELSM Unreviewed; 265 AA.
AC F2I0M4;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanine ligase {ECO:0000313|EMBL:AEA81229.1};
DE EC=6.3.2.10 {ECO:0000313|EMBL:AEA81229.1};
GN OrderedLocusNames=SAR11G3_00754 {ECO:0000313|EMBL:AEA81229.1};
OS Pelagibacter sp. (strain IMCC9063).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae; Pelagibacter.
OX NCBI_TaxID=1002672 {ECO:0000313|EMBL:AEA81229.1, ECO:0000313|Proteomes:UP000009181};
RN [1] {ECO:0000313|EMBL:AEA81229.1, ECO:0000313|Proteomes:UP000009181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC9063 {ECO:0000313|EMBL:AEA81229.1,
RC ECO:0000313|Proteomes:UP000009181};
RX PubMed=21515764; DOI=10.1128/JB.05033-11;
RA Oh H.M., Kang I., Lee K., Jang Y., Lim S.I., Cho J.C.;
RT "Complete genome sequence of strain IMCC9063, belonging to SAR11 subgroup
RT 3, isolated from the Arctic Ocean.";
RL J. Bacteriol. 193:3379-3380(2011).
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DR EMBL; CP002511; AEA81229.1; -; Genomic_DNA.
DR RefSeq; WP_013695394.1; NC_015380.1.
DR AlphaFoldDB; F2I0M4; -.
DR STRING; 1002672.SAR11G3_00754; -.
DR KEGG; pel:SAR11G3_00754; -.
DR eggNOG; COG0770; Bacteria.
DR HOGENOM; CLU_1049085_0_0_5; -.
DR OrthoDB; 9800958at2; -.
DR Proteomes; UP000009181; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008766; F:UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-EC.
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; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR Gene3D; 3.40.1390.10; MurE/MurF, N-terminal domain; 1.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR InterPro; IPR000713; Mur_ligase_N.
DR InterPro; IPR035911; MurE/MurF_N.
DR PANTHER; PTHR43024; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR PANTHER; PTHR43024:SF1; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR Pfam; PF01225; Mur_ligase; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF63418; MurE/MurF N-terminal domain; 1.
PE 4: Predicted;
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:0000313|EMBL:AEA81229.1};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000009181}.
FT DOMAIN 23..70
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 108..257
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
SQ SEQUENCE 265 AA; 30326 MW; 90E38C7B17A92601 CRC64;
MNINSIDLQK IFNKEILNKK ININNVTINS KEVTAKSIFF AIKGKNTDGH YFVKEVIKKR
SKVIVVKNNF KVPKNNLHKF IKVRSPIRSL ENFAKYQRLT SQGKFVGITG SFGKTTLKYM
LSFFLEQYGK TFSSPKSFNN HFGLPLSLSN TPKNSQFNIF ELGMSSSREI DKLSQILRPD
IGVITNIGPA HLKNFKNLKA VCLAKAEIMN HIQENGYIVL NKDDFYFNTL FKIANNKKLK
IITFSKSKKA NVQLLKIIKK KIVIK
//
