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Database: UniProt
Entry: A0A1I5C087_9PROT
LinkDB: A0A1I5C087_9PROT
Original site: A0A1I5C087_9PROT 
ID   A0A1I5C087_9PROT        Unreviewed;       471 AA.
AC   A0A1I5C087;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136};
DE            EC=6.3.2.10 {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136};
DE   AltName: Full=D-alanyl-D-alanine-adding enzyme {ECO:0000256|HAMAP-Rule:MF_02019};
GN   Name=murF {ECO:0000256|HAMAP-Rule:MF_02019};
GN   ORFNames=SAMN05216386_1886 {ECO:0000313|EMBL:SFN80021.1};
OS   Nitrosospira briensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=35799 {ECO:0000313|EMBL:SFN80021.1, ECO:0000313|Proteomes:UP000183107};
RN   [1] {ECO:0000313|Proteomes:UP000183107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nsp8 {ECO:0000313|Proteomes:UP000183107};
RA   Varghese N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in cell wall formation. Catalyzes the final step in
CC       the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of
CC       murein. {ECO:0000256|HAMAP-Rule:MF_02019,
CC       ECO:0000256|RuleBase:RU004136}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-
CC         alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate = ADP + H(+) +
CC         phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-
CC         meso-2,6-diaminopimeloyl-D-alanyl-D-alanine; Xref=Rhea:RHEA:28374,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57822, ChEBI:CHEBI:61386, ChEBI:CHEBI:83905,
CC         ChEBI:CHEBI:456216; EC=6.3.2.10; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02019, ECO:0000256|RuleBase:RU004136};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019,
CC       ECO:0000256|RuleBase:RU004136}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. MurF subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02019}.
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DR   EMBL; FOVJ01000003; SFN80021.1; -; Genomic_DNA.
DR   RefSeq; WP_074796908.1; NZ_FOVJ01000003.1.
DR   AlphaFoldDB; A0A1I5C087; -.
DR   OrthoDB; 9801978at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000183107; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-UniRule.
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-UniRule.
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; 3.40.1390.10; MurE/MurF, N-terminal domain; 1.
DR   HAMAP; MF_02019; MurF; 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   InterPro; IPR035911; MurE/MurF_N.
DR   InterPro; IPR005863; UDP-N-AcMur_synth.
DR   NCBIfam; TIGR01143; murF; 1.
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; 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.
DR   SUPFAM; SSF63418; MurE/MurF N-terminal domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02019};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_02019};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_02019};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_02019};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_02019};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000313|EMBL:SFN80021.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02019};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_02019}; Reference proteome {ECO:0000313|Proteomes:UP000183107}.
FT   DOMAIN          22..98
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          108..307
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          328..404
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
FT   BINDING         110..116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02019"
SQ   SEQUENCE   471 AA;  50123 MW;  C253FD7F4079D25A CRC64;
     MMTVQEAARA LHGDWSGEDA YFTGVGTDSR SVRQGDLFVA LTGPAFDGHD FIAEVAEKGA
     AAAMVHRDAG AKIRESGIPL IRVENTRLAL GQLAAHWRGR FSMPVVAVTG SNGKTTVKEM
     IASILRCVAG QAEPLKGHLS GSDKVLATEG NLNNDIGVPL MLLRLREWHR YVVMEMGMNH
     AGEISYLTGL VKPDVALITN AGEAHVEGLG SVEAVARAKG EVFEGLGQHG VAVINADDPH
     APLWRRLAGD RKVVDFGLEG EPAVGARYQP GVLDSRVTLN LPDGVEEVKL QVPGEHNVRN
     ALAAAAAGVA LGIGAKAIVS GLTAFRGVKG RLQKKRGLHD AALIDDSYNA NPDSVRAALA
     VLAKAEGKKI FVFGDMGELG SGARDFHERV GTEARAAGID RLLALGKLSA YTVEKFGSGA
     RHFKNIQDLL TEVESLLGRD VTLLVKGSRF MQMERVVRHI ELPGTDKTDE P
//
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