Reviewed, UniProtKB/Swiss-Prot Q9WY73 (MURC_THEMA)

Names and origin

Protein names

Recommended name:
    UDP-N-acetylmuramate--L-alanine ligase
    EC=6.3.2.8
Alternative name(s):
    UDP-N-acetylmuramoyl-L-alanine synthetase

Gene names

Name:	murC
Ordered Locus Names:	TM_0231

Organism

Thermotoga maritima [Complete proteome] [HAMAP]

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	457 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Cell wall formation. HAMAP MF_00046
Catalytic activity	ATP + UDP-N-acetylmuramate + L-alanine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine. HAMAP MF_00046
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00046
Subcellular location	Cytoplasm Probable HAMAP MF_00046.
Sequence similarities	Belongs to the murCDEF family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP UDP-N-acetylmuramate-L-alanine ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 457

457

UDP-N-acetylmuramate--L-alanine ligase HAMAP MF_00046

PRO_0000182177

Regions

Nucleotide binding

109 – 115

7

ATP Potential

Secondary structure

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457

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Turn

7 – 9

3

Helix

11 – 22

12

Beta strand

26 – 30

5

Helix

36 – 43

8

Beta strand

48 – 51

4

Beta strand

61 – 65

5

Helix

74 – 81

8

Beta strand

86 – 88

3

Helix

89 – 100

12

Beta strand

104 – 108

5

Beta strand

110 – 112

3

Helix

113 – 126

14

Beta strand

132 – 134

3

Beta strand

145 – 148

4

Beta strand

154 – 158

5

Helix

163 – 167

5

Beta strand

171 – 175

5

Helix

183 – 186

4

Helix

190 – 202

13

Beta strand

205 – 210

6

Turn

214 – 216

3

Helix

217 – 219

3

Beta strand

221 – 224

4

Beta strand

226 – 238

13

Beta strand

243 – 249

7

Beta strand

252 – 261

10

Helix

264 – 279

16

Helix

284 – 293

10

Beta strand

300 – 307

8

Turn

308 – 311

4

Beta strand

312 – 317

6

Helix

322 – 335

14

Beta strand

337 – 345

9

Helix

359 – 364

6

Beta strand

367 – 372

6

Helix

388 – 397

10

Beta strand

402 – 404

3

Helix

408 – 410

3

Helix

411 – 414

4

Beta strand

419 – 426

8

Helix

431 – 445

15

Sequences

	Sequence		Length	Mass (Da)
	Q9WY73-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 7D9AEDC50482351D	FASTA	457	51,872
	10 20 30 40 50 60 MKIHFVGIGG IGMSAVALHE FSNGNDVYGS NIEETERTAY LRKLGIPIFV PHSADNWYDP 70 80 90 100 110 120 DLVIKTPAVR DDNPEIVRAR MERVPIENRL HYFRDTLKRE KKEEFAVTGT DGKTTTTAMV 130 140 150 160 170 180 AHVLKHLRKS PTVFLGGIMD SLEHGNYEKG NGPVVYELDE SEEFFSEFSP NYLIITNARG 190 200 210 220 230 240 DHLENYGNSL TRYRSAFEKI SRNTDLVVTF AEDELTSHLG DVTFGVKKGT YTLEMRSASR 250 260 270 280 290 300 AEQKAMVEKN GKRYLELKLK VPGFHNVLNA LAVIALFDSL GYDLAPVLEA LEEFRGVHRR 310 320 330 340 350 360 FSIAFHDPET NIYVIDDYAH TPDEIRNLLQ TAKEVFENEK IVVIFQPHRY SRLEREDGNF 370 380 390 400 410 420 AKALQLADEV VVTEVYDAFE EKKNGISGKM IWDSLKSLGK EAYFVEKLPE LEKVISVSEN 430 440 450 TVFLFVGAGD IIYSSRRFVE RYQSSKSSPS RVLGSNK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Nature 399:323-329(1999) [PubMed: 10360571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]	"Crystal structure of an UDP-N-acetylmuramate-alanine ligase MurC (TM0231) from Thermotoga maritima at 2.3-A resolution." Spraggon G., Schwarzenbacher R., Kreusch A., Lee C.C., Abdubek P., Ambing E., Biorac T., Brinen L.S., Canaves J.M., Cambell J., Chiu H.-J., Dai X., Deacon A.M., DiDonato M., Elsliger M.-A., Eshagi S., Floyd R., Godzik A. , Grittini C., Grzechnik S.K., Hampton E., Jaroszewski L., Karlak C., Klock H.E., Koesema E., Kovarik J.S., Kuhn P., Levin I., McMullan D., McPhillips T.M., Miller M.D., Morse A., Moy K., Ouyang J., Page R., Quijano K., Robb A., Stevens R.C., van den Bedem H., Velasquez J., Vincent J., von Delft F., Wang X., West B., Wolf G., Xu Q., Hodgson K.O., Wooley J., Lesley S.A., Wilson I.A. Proteins 55:1078-1081(2004) [PubMed: 15146505] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000512 Genomic DNA. Translation: AAD35322.1.

PIR

A72402.

RefSeq

NP_228045.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1J6U	X-ray	2.30	A	1-457	[»]

ModBase

Search...

Genome annotation databases

GeneID

897130.

GenomeReviews

Gene locus TM_0231 in contig AE000512_GR.

KEGG

tma:TM0231.

NMPDR

fig|243274.1.peg.229.

TIGR

TM_0231.

Phylogenomic databases

HOGENOM

HBG476594.

OMA

YQPHRYS.

Enzyme and pathway databases

BioCyc

TMAR243274:TM_0231-MONOMER.

BRENDA

6.3.2.8. 16699.

Family and domain databases

HAMAP

MF_00046. MurC.
[Tree]

InterPro

IPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
IPR000713. Mur_ligase_N.
IPR016040. NAD(P)-bd_dom.
IPR005758. UDP-N-AcMur_Ala_ligase.
[Graphical view]

Gene3D

G3DSA:3.90.190.20. Mur_ligase_C. 1 hit.
G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit.
G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

Pfam

PF01225. Mur_ligase. 1 hit.
PF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01082. murC. 1 hit.

ProtoNet

Search...

Entry information

Entry name

MURC_THEMA

Accession

Primary (citable) accession number: Q9WY73

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1999
Last modified:	February 9, 2010
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)