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Database: UniProt
Entry: A0A017RSZ8_9CLOT
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Original site: A0A017RSZ8_9CLOT 
ID   A0A017RSZ8_9CLOT        Unreviewed;       456 AA.
AC   A0A017RSZ8;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 48.
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   ORFNames=Q428_10690 {ECO:0000313|EMBL:EYE87888.1};
OS   Fervidicella metallireducens AeB.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Fervidicella.
OX   NCBI_TaxID=1403537 {ECO:0000313|EMBL:EYE87888.1, ECO:0000313|Proteomes:UP000019681};
RN   [1] {ECO:0000313|EMBL:EYE87888.1, ECO:0000313|Proteomes:UP000019681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AeB {ECO:0000313|EMBL:EYE87888.1,
RC   ECO:0000313|Proteomes:UP000019681};
RX   PubMed=24786951;
RA   Patel B.K.;
RT   "Draft Genome Sequence of Fervidicella metallireducens Strain AeBT, an
RT   Iron-Reducing Thermoanaerobe from the Great Artesian Basin.";
RL   Genome Announc. 2:e00345-14(2014).
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|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00046}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00046}.
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:EYE87888.1}.
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DR   EMBL; AZQP01000034; EYE87888.1; -; Genomic_DNA.
DR   RefSeq; WP_035380621.1; NZ_AZQP01000034.1.
DR   AlphaFoldDB; A0A017RSZ8; -.
DR   STRING; 1403537.Q428_10690; -.
DR   OrthoDB; 9804126at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000019681; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
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}; Reference proteome {ECO:0000313|Proteomes:UP000019681};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          11..109
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          115..293
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          315..396
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
FT   BINDING         117..123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00046"
SQ   SEQUENCE   456 AA;  50389 MW;  3AB1CEB0943EC6DE CRC64;
     MFDIYNDKNK KVHFIGIGGI SMSGLAEILI DYGYHVSGSD RSKSKFTDKL QKLGADIFIG
     HEPSHVHGAD LVVYTAAVKD DNPELIEAKN LDIPLMDRAE FLGAIMKKFS KGIAVSGTHG
     KTTVTSMIST VLLNADLDPT IMVGGELDAI DGNVKPGKSP YFITEACEYK GSFLKFYPYI
     GIILNIDADH LDYYKDIKEI HDTFFAFADL IPKDGLLIGC AEDDRVIDIC KKVKCNTLTY
     GIKHGDFTAK DIVYDSKGFP SFTACYKGED YGRFSLSVPG EHNVLNALSA IACSYFLGID
     KDVTAASLKS FTGTHRRFEK KGEKNGVVVI DDYAHHPAEI IATIKAAKNY PHKRIFCVFQ
     PHTYTRTYTL FEDFAKAFNG LDKLILTDIY AAREKDTGLV SSNKLCEAVK NYGVNAVHIS
     SFKEIVEDLS NELKEGDLLI TMGAGDVYLV GEDYLK
//
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