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Multifunctional fusion protein [Includes: UDP-N-acetylmuramate--L-alanine ligase (EC 6.3.2.8) (UDP-N-acetylmuramoyl-L-alanine synthetase); D-alanine--D-alanine ligase (EC 6.3.2.4) (D-Ala-D-Ala ligase) (D-alanylalanine synthetase)]

 S7K4D7_CHLPS            Unreviewed;       810 AA.
S7K4D7;
16-OCT-2013, integrated into UniProtKB/TrEMBL.
16-OCT-2013, sequence version 1.
05-DEC-2018, entry version 47.
RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|HAMAP-Rule:MF_00047};
Includes:
RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00047};
EC=6.3.2.4 {ECO:0000256|HAMAP-Rule:MF_00047};
AltName: Full=D-Ala-D-Ala ligase {ECO:0000256|HAMAP-Rule:MF_00047};
AltName: Full=D-alanylalanine synthetase {ECO:0000256|HAMAP-Rule:MF_00047};
Includes:
RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00046};
EC=6.3.2.8 {ECO:0000256|HAMAP-Rule:MF_00046};
AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase {ECO:0000256|HAMAP-Rule:MF_00046};
Name=murC {ECO:0000256|HAMAP-Rule:MF_00046,
ECO:0000313|EMBL:EPP29445.1};
Synonyms=ddl {ECO:0000256|HAMAP-Rule:MF_00047};
ORFNames=CP082626L3_1148 {ECO:0000313|EMBL:EPP29445.1};
Chlamydia psittaci 08-2626_L3.
Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
Chlamydia/Chlamydophila group; Chlamydia.
NCBI_TaxID=1112246 {ECO:0000313|EMBL:EPP29445.1};
[1] {ECO:0000313|EMBL:EPP29445.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=08-2626_L3 {ECO:0000313|EMBL:EPP29445.1};
Huot-Creasy H., McCracken C.L., Humphries M., Sachse K., Laroucau K.,
Bavoil P., Myers G.S.;
"Genome sequence of Chlamydia psittaci 08-2626 L3.";
Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00047}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) +
phosphate; Xref=Rhea:RHEA:11224, ChEBI:CHEBI:15378,
ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57416,
ChEBI:CHEBI:57822, ChEBI:CHEBI:456216; EC=6.3.2.4;
Evidence={ECO:0000256|HAMAP-Rule:MF_00047};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP +
H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine;
Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757,
ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8;
Evidence={ECO:0000256|HAMAP-Rule:MF_00046,
ECO:0000256|SAAS:SAAS00382229};
-!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
{ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00382155}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047,
ECO:0000256|SAAS:SAAS00382163}.
-!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
{ECO:0000256|HAMAP-Rule:MF_00047}.
-!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000256|HAMAP-
Rule:MF_00046}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:EPP29445.1}.
-----------------------------------------------------------------------
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EMBL; ATMX01000130; EPP29445.1; -; Genomic_DNA.
RefSeq; WP_006343520.1; NZ_KE360760.1.
EnsemblBacteria; EPP29445; EPP29445; CP082626L3_1148.
GeneID; 12243322; -.
PATRIC; fig|1112246.4.peg.388; -.
OrthoDB; POG091H02MF; -.
UniPathway; UPA00219; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:InterPro.
GO; GO:0008763; F:UDP-N-acetylmuramate-L-alanine ligase activity; IEA:UniProtKB-UniRule.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
Gene3D; 3.30.1490.20; -; 1.
Gene3D; 3.40.1190.10; -; 1.
Gene3D; 3.90.190.20; -; 1.
HAMAP; MF_00047; Dala_Dala_lig; 1.
HAMAP; MF_00046; MurC; 1.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR000291; D-Ala_lig_Van_CS.
InterPro; IPR005905; D_ala_D_ala.
InterPro; IPR011095; Dala_Dala_lig_C.
InterPro; IPR011127; Dala_Dala_lig_N.
InterPro; IPR036565; Mur-like_cat_sf.
InterPro; IPR004101; Mur_ligase_C.
InterPro; IPR036615; Mur_ligase_C_dom_sf.
InterPro; IPR013221; Mur_ligase_cen.
InterPro; IPR000713; Mur_ligase_N.
InterPro; IPR016185; PreATP-grasp_dom_sf.
InterPro; IPR005758; UDP-N-AcMur_Ala_ligase_murC.
Pfam; PF07478; Dala_Dala_lig_C; 1.
Pfam; PF01820; Dala_Dala_lig_N; 1.
Pfam; PF01225; Mur_ligase; 1.
Pfam; PF02875; Mur_ligase_C; 1.
Pfam; PF08245; Mur_ligase_M; 1.
SUPFAM; SSF52440; SSF52440; 1.
SUPFAM; SSF53244; SSF53244; 1.
SUPFAM; SSF53623; SSF53623; 1.
TIGRFAMs; TIGR01205; D_ala_D_alaTIGR; 1.
TIGRFAMs; TIGR01082; murC; 1.
PROSITE; PS50975; ATP_GRASP; 1.
PROSITE; PS00843; DALA_DALA_LIGASE_1; 1.
PROSITE; PS00844; DALA_DALA_LIGASE_2; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|PROSITE-
ProRule:PRU00409, ECO:0000256|SAAS:SAAS00084995};
Cell cycle {ECO:0000256|HAMAP-Rule:MF_00046,
ECO:0000256|SAAS:SAAS00085032};
Cell division {ECO:0000256|HAMAP-Rule:MF_00046,
ECO:0000256|SAAS:SAAS00085032};
Cell shape {ECO:0000256|HAMAP-Rule:MF_00047,
ECO:0000256|SAAS:SAAS00085152};
Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00047,
ECO:0000256|SAAS:SAAS00085135};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047,
ECO:0000256|SAAS:SAAS00085104};
Ligase {ECO:0000256|HAMAP-Rule:MF_00047,
ECO:0000256|SAAS:SAAS00085127, ECO:0000313|EMBL:EPP29445.1};
Membrane {ECO:0000256|SAM:Phobius};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00046,
ECO:0000256|PROSITE-ProRule:PRU00409, ECO:0000256|SAAS:SAAS00084995};
Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00047,
ECO:0000256|SAAS:SAAS00085152};
Transmembrane {ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAM:Phobius}.
TRANSMEM 7 25 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 573 784 ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
NP_BIND 111 117 ATP. {ECO:0000256|HAMAP-Rule:MF_00046}.
SEQUENCE 810 AA; 91033 MW; 9E393F8C94556C34 CRC64;
MDRKIHYHFI GIGGIGMSAL AHILLDRGYS VSGSDLNRGA IIDKLVAKGA RYLQGHDKHH
IPEDCTIIYG SGIAKDNVEY LEAVRKQLPI LHRSELLAFL MQEQTSILVS GSHGKTTVSS
LITAIFQTAK KDPSYAIGGL NSLSLNGYSG SSEYFIAEAD ESDGSLKHYL PKVAVVTNLD
NEHLSNFEGS KEKLALTIEE FTRKVEDPRL CFYNGDCQEL KGRISGTSYG FSQDCNLRIH
SYYQDGWRSL FSLSFLGKDY LDIDLNLIGK HNIANAAVAM GIALTLGIDE ESIREALKNF
SGIQRRMERK NVSEKFLFFE DYAHHPSEIS CTLRGLRDAV GLRRIVAICQ PHRFSRLQYC
LEDFYKAFQD ADEVILTDVY SAGETALDLP SPEKLAETIS LSSHVQCSYV PYDNIIPYLQ
QEIRVHDVCI SLGAGNIYTV GNALKDFEPR KLAVGVVCGG KSCEHDISLL SARNVVRYLS
PEYYDVQYFI IDRQGLWSKV STIECEDYEG KGHYVLSSEI TEALTHVDFI LPILHGPFGE
DGTLQGFLEI INKPYAGPSL LFSSVTMDKI MTKRLAASVG VPVVPYQPLT LHAWKRTPEL
CMHKISEAFT FPMFVKTAHL GSSIGVFEVH NEEELKAKIS EAFLYDTDIF IEESRLGSRE
IEVSCLGDSS SCYYISEPHE RCGEKRFISY EEKYGLNGRA SAQIQYDLDL SEESKIRVKE
FTERVYRVIQ GQGSCRVDFF LDDEGNFWLS EMNPIPGMTQ ASPFLHDFAR LGWTFEQIIH
QLIISGLHKF DRKKKVGKTL NKQCLLTAKS


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