P17893 (ARGR_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Arginine repressor

Alternative name(s):
Arginine hydroxamate resistance protein

Gene names

Name:	argR
Synonyms:	ahrC
Ordered Locus Names:	BSU24250

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	149 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Represses the synthesis of biosynthetic enzymes and activates the arginine catabolism. Controls the transcription of the two operons rocABC and rocDEF. HAMAP MF_00173
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis. [regulation] HAMAP MF_00173 Amino-acid degradation; L-arginine degradation via ADI pathway. HAMAP MF_00173
Subunit structure	Homohexamer.
Subcellular location	Cytoplasm HAMAP MF_00173.
Sequence similarities	Belongs to the ArgR family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis Arginine metabolism Transcription Transcription regulation
Cellular component	Cytoplasm
Ligand	DNA-binding
Molecular function	Repressor
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 149

149

Arginine repressor HAMAP MF_00173

PRO_0000205072

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

149

Helix Strand Turn

Details...

Helix

3 – 16

14

Helix

22 – 31

10

Helix

38 – 48

11

Beta strand

51 – 55

5

Turn

56 – 58

3

Beta strand

59 – 63

5

Helix

72 – 83

12

Beta strand

84 – 89

6

Beta strand

91 – 99

9

Helix

103 – 111

9

Beta strand

118 – 123

6

Beta strand

125 – 134

10

Helix

135 – 146

12

Sequences

	Sequence		Length	Mass (Da)
	P17893 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: 3608F3B023FCC293	FASTA	149	16,832
	10 20 30 40 50 60 MNKGQRHIKI REIITSNEIE TQDELVDMLK QDGYKVTQAT VSRDIKELHL VKVPTNNGSY 70 80 90 100 110 120 KYSLPADQRF NPLSKLKRAL MDAFVKIDSA SHMIVLKTMP GNAQAIGALM DNLDWDEMMG 130 140 TICGDDTILI ICRTPEDTEG VKNRLLELL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of a Bacillus subtilis arginine regulatory gene and homology of its product to the Escherichia coli arginine repressor." North A.K., Smith M.C.M., Baumberg S. Gene 80:29-38(1989) [PubMed: 2507400] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes." Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y. Microbiology 142:3103-3111(1996) [PubMed: 8969508] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / JH642.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"Characterization of the spoIVB and recN loci of Bacillus subtilis." van Hoy B.E., Hoch J.A. J. Bacteriol. 172:1306-1311(1990) [PubMed: 2106508] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 120-149.
[5]	"Purification and initial characterization of AhrC: the regulator of arginine metabolism genes in Bacillus subtilis." Czaplewski L.G., North A.K., Smith M.C.M., Baumberg S., Stockley P.G. Mol. Microbiol. 6:267-275(1992) [PubMed: 1312212] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-30.
[6]	"The structure of AhrC, the arginine repressor/activator protein from Bacillus subtilis." Dennis C.A., Glykos N.M., Parsons M.R., Phillips S.E. Acta Crystallogr. D 58:421-430(2002) [PubMed: 11856827] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M27869 Genomic DNA. Translation: AAA22208.1.
D84432 Genomic DNA. Translation: BAA12578.1.
AL009126 Genomic DNA. Translation: CAB14356.1.
M30297 Genomic DNA. Translation: AAA22690.1.

PIR

JS0275.

RefSeq

NP_390305.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F9N	X-ray	2.70	A/B/C/D/E/F	1-149	[»]
2P5K	X-ray	1.00	A	1-64	[»]
2P5L	X-ray	2.85	C/D/G/H	1-64	[»]
2P5M	X-ray	1.95	A/B/C	68-149	[»]

ProteinModelPortal

P17893.

SMR

P17893. Positions 1-149.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBBACT00000001650; EBBACP00000001650; EBBACG00000001648.

GeneID

938653.

GenomeReviews

Gene locus BSU24250 in contig AL009126_GR.

KEGG

bsu:BSU24250.

NMPDR

fig|224308.1.peg.2429.

PATRIC

18976684. VBIBacSub10457_2532.

Organism-specific databases

GenoList

BSU24250. [Micado]

Phylogenomic databases

GeneTree

EBGT00050000001828.

HOGENOM

HBG697909.

OMA

ASAIDHS.

PhylomeDB

P17893.

ProtClustDB

PRK04280.

Enzyme and pathway databases

BioCyc

BSUB:BSU24250-MONOMER.

Family and domain databases

HAMAP

MF_00173. Arg_repressor.
[Tree]

InterPro

IPR001669. Arg_repress.
IPR020899. Arg_repress_C.
IPR020900. Arg_repress_DNA-bd.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]

Gene3D

G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.

KO

K03402.

Pfam

PF01316. Arg_repressor. 1 hit.
PF02863. Arg_repressor_C. 1 hit.
[Graphical view]

PRINTS

PR01467. ARGREPRESSOR.

ProDom

PD007402. Arg_repress. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF55252. Arg_repress. 1 hit.

TIGRFAMs

TIGR01529. ArgR_whole. 1 hit.

ProtoNet

Search...

Entry information

Entry name

ARGR_BACSU

Accession

Primary (citable) accession number: P17893

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	January 25, 2012
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program