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Database: UniProt
Entry: A0A068YVZ7_9GAMM
LinkDB: A0A068YVZ7_9GAMM
Original site: A0A068YVZ7_9GAMM 
ID   A0A068YVZ7_9GAMM        Unreviewed;       491 AA.
AC   A0A068YVZ7;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0000256|ARBA:ARBA00012211, ECO:0000256|HAMAP-Rule:MF_00046};
DE            EC=6.3.2.8 {ECO:0000256|ARBA:ARBA00012211, ECO:0000256|HAMAP-Rule:MF_00046};
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase {ECO:0000256|HAMAP-Rule:MF_00046};
GN   Name=murC {ECO:0000256|HAMAP-Rule:MF_00046,
GN   ECO:0000313|EMBL:MXR54195.1};
GN   ORFNames=GPZ83_006690 {ECO:0000313|EMBL:NYV29694.1}, GPZ83_05700
GN   {ECO:0000313|EMBL:MXR54195.1}, SYMBAF_13645
GN   {ECO:0000313|EMBL:QLH63770.1};
OS   Serratia symbiotica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=138074 {ECO:0000313|EMBL:MXR54195.1};
RN   [1] {ECO:0000313|EMBL:QLH63770.1, ECO:0000313|Proteomes:UP000042738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CWBI-2.3 {ECO:0000313|EMBL:QLH63770.1};
RX   PubMed=25146134;
RA   Foray V., Grigorescu A.S., Sabri A., Haubruge E., Lognay G., Francis F.,
RA   Fauconnier M.L., Hance T., Thonart P.;
RT   "Whole-Genome Sequence of Serratia symbiotica Strain CWBI-2.3T, a Free-
RT   Living Symbiont of the Black Bean Aphid Aphis fabae.";
RL   Genome Announc. 2:e00767-e00714(2014).
RN   [2] {ECO:0000313|EMBL:QLH63770.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CWBI-2.3 {ECO:0000313|EMBL:QLH63770.1};
RA   Foray V.V.;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:MXR54195.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=24.1 {ECO:0000313|EMBL:MXR54195.1};
RA   Renoz F., Ambroise J., Gala J.-L., Hance T.;
RT   "Draft genome sequence of Serratia symbiotica strain 24.1.";
RL   Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:NYV29694.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=24.1 {ECO:0000313|EMBL:NYV29694.1}, and CWBI-2.3
RC   {ECO:0000313|EMBL:QLH63770.1};
RA   Renoz F., Foray V., Ambroise J., Baa-Puyoulet P., Bearzatto B.,
RA   Mendez G.L., Vanderpoorten A., Mahillon J., Gala J.-L., Calevro F.,
RA   Hance T.;
RT   "Genomic Insight into Nascent Stage of Mutualistic Insect Bacterial
RT   Symbioses through the Bacterial Symbiont Serratia symbiotica.";
RL   Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00046}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) +
CC         phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine;
CC         Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757,
CC         ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00001677, ECO:0000256|HAMAP-
CC         Rule:MF_00046};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00046}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00046}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00046}.
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DR   EMBL; WSPN01000010; MXR54195.1; -; Genomic_DNA.
DR   EMBL; WSPN02000002; NYV29694.1; -; Genomic_DNA.
DR   EMBL; CP050855; QLH63770.1; -; Genomic_DNA.
DR   STRING; 138074.SYMBAF_10144; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000042738; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008763; F:UDP-N-acetylmuramate-L-alanine ligase activity; IEA:UniProtKB-UniRule.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00046; MurC; 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; IPR005758; UDP-N-AcMur_Ala_ligase_MurC.
DR   NCBIfam; TIGR01082; murC; 1.
DR   PANTHER; PTHR43445:SF3; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE; 1.
DR   PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00046};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_00046};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_00046};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_00046};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_00046};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00046};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00046};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00046};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_00046}.
FT   DOMAIN          21..119
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          124..304
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          343..417
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
FT   BINDING         126..132
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00046"
SQ   SEQUENCE   491 AA;  53359 MW;  A2E14A7F2C972207 CRC64;
     MNTQQLAKLR TIVPEMRRVR HIHFVGIGGA GMGGIAEVLA NEGYQISGSD LAPNPVTQQL
     SALGATIYFN HRTENVLDAS VVVVSSAISA DNPEIVAARE ARIPVIRRAE MLAELMRFRH
     GIAVAGTHGK TTTTAMVSSI YAEADLDPTF VNGGLVKAAG THARLGSSRF LIAEADESDA
     SFLHLQPMVA IITNIEADHM DTYQGDFENL KQTFINFLHN LPFYGRAVMC IDDPVVRELL
     PCVGRHITTY GFSNDADVRI ENYHQLGAQG CFTLSRQDKP LITVTLNAPG RHNALNAAAA
     AAVATEEGID DEDILRALAS FQGTGRRFDF LGEFPLATVN GKAGSAMLVD DYGHHPTEVD
     ATLQAARAGW PDKRLVMIFQ PHRYTRTRDL YDDFANVLSQ VDVLLMLEVY AAGETPIPGA
     DSRALCRTIR SRGKLDPILV SDADSVPEIL AQLLQADDLV LVQGAGNVGK IARKLAEVKL
     QPQKKEEEYH G
//
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