Q02147 (HISZ_LACLA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP phosphoribosyltransferase regulatory subunit

Gene names

Name:	hisZ
Ordered Locus Names:	LL1207
ORF Names:	L0341

Organism

Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)

Taxonomic identifier

272623 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Lactococcus

Protein attributes

Sequence length	328 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine. HAMAP MF_00125
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. HAMAP MF_00125
Subunit structure	Heterooctamer composed of four hisG and four hisZ subunits Probable. Ref.4
Subcellular location	Cytoplasm Probable HAMAP MF_00125.
Miscellaneous	This function is generally fulfilled by the C-terminal part of hisG, which is missing in some bacteria such as this one. HAMAP MF_00125 The stability and homogeneity of the hisG-hisZ complex is apparently increased by ATP and 5-phosphoribose 1-diphosphate but decreased in the presence of the regulatory inhibitor histidine. HAMAP MF_00125
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. HisZ subfamily.
Sequence caution	The sequence AAK05305.1 differs from that shown. Reason: Frameshift at position 38.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Cellular component	Cytoplasm
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW histidyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro histidine-tRNA ligase 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 – 328

328

ATP phosphoribosyltransferase regulatory subunit HAMAP MF_00125

PRO_0000171038

Experimental info

Sequence conflict

73

1

K → N in AAB81902. Ref.1

Sequence conflict

174

1

Q → H in AAB81902. Ref.1

Sequence conflict

210

1

G → E in AAB81902. Ref.1

Sequence conflict

303

1

F → V in AAB81902. Ref.1

Secondary structure

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328

Helix Strand Turn

Details...

Helix

17 – 36

20

Beta strand

46 – 49

4

Helix

50 – 57

8

Beta strand

59 – 61

3

Beta strand

70 – 72

3

Beta strand

78 – 81

4

Helix

86 – 94

9

Beta strand

102 – 109

8

Beta strand

125 – 134

10

Helix

136 – 154

19

Beta strand

157 – 165

9

Helix

166 – 175

10

Turn

176 – 178

3

Helix

180 – 188

9

Helix

192 – 199

8

Helix

206 – 215

10

Helix

221 – 230

10

Helix

234 – 250

17

Turn

251 – 253

3

Beta strand

271 – 278

8

Beta strand

281 – 290

10

Helix

292 – 296

5

Beta strand

298 – 300

3

Beta strand

305 – 310

6

Helix

311 – 322

12

Sequences

	Sequence		Length	Mass (Da)
	Q02147 [UniParc]. Last modified May 15, 2002. Version 2. Checksum: 2B47DC880331580D	FASTA	328	37,943
	10 20 30 40 50 60 MEKINYLLPE ESAEMTLNQV KSLRQIEGRL RKLFSLKNYQ EVMPPSFEYT QLYTALESNG 70 80 90 100 110 120 KTFNQEKMFQ FIKHEGQSIT LRYDFTLPLV RLYSQIKDST SARYSYFGKI FRKEKRHKGR 130 140 150 160 170 180 STENYQIGIE LFGESADKSE LEILSLALQV IEQLGLNKTV FEIGSAKFFQ RLCQLADGST 190 200 210 220 230 240 ELLTELLLKK DLSGLNAFIE KNNFSKELRG LLKEIFITNE LSRLENLVTN TKDDVLISSF 250 260 270 280 290 300 DQLKEFSEKL SMIKPIIIDL GMVPKMDYYT DLMFKAYSSA ANQPILSGGR YDQLLSNFQE 310 320 EAFAIGFCCH MDTILKALER QELEEDND

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Histidine biosynthesis genes in Lactococcus lactis subsp. lactis." Delorme C., Ehrlich S.D., Renault P. J. Bacteriol. 174:6571-6579(1992) [PubMed: 1400209] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: NCDO 2118.
[2]	"The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403." Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J., Ehrlich S.D., Sorokin A. Genome Res. 11:731-753(2001) [PubMed: 11337471] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: IL1403.
[3]	"An aminoacyl-tRNA synthetase paralog with a catalytic role in histidine biosynthesis." Sissler M., Delorme C., Bond J., Ehrlich S.D., Renault P., Francklyn C. Proc. Natl. Acad. Sci. U.S.A. 96:8985-8990(1999) [PubMed: 10430882] [Abstract] Cited for: CHARACTERIZATION.
[4]	"The quaternary structure of the HisZ-HisG N-1-(5'-phosphoribosyl)-ATP transferase from Lactococcus lactis." Bovee M.L., Champagne K.S., Demeler B., Francklyn C.S. Biochemistry 41:11838-11846(2002) [PubMed: 12269828] [Abstract] Cited for: SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U92974 Genomic DNA. Translation: AAB81902.1.
AE005176 Genomic DNA. Translation: AAK05305.1. Frameshift.

PIR

C45734.
G86775.

RefSeq

NP_267363.1. NC_002662.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Z7M	X-ray	2.90	A/B/C/D	1-328	[»]
1Z7N	X-ray	3.25	A/B/C/D	1-328	[»]

ProteinModelPortal

Q02147.

SMR

Q02147. Positions 6-323.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1114854.

GenomeReviews

Gene locus LL1207 in contig AE005176_GR.

KEGG

lla:L0341.

NMPDR

fig|272623.1.peg.1242.

PATRIC

22294788. VBILacLac136773_1302.

Phylogenomic databases

HOGENOM

HBG517872.

ProtClustDB

CLSK697628.

Enzyme and pathway databases

BioCyc

LLAC272623:L0341-MONOMER.

Family and domain databases

HAMAP

MF_00125. HisZ.
[Tree]

InterPro

IPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004516. His-tRNA_synth_IIA.
[Graphical view]

KO

K02502.

PANTHER

PTHR11476. His-tRNA_synth. 1 hit.

Pfam

PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]

PIRSF

PIRSF001549. His-tRNA_synth. 1 hit.

PROSITE

PS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

HISZ_LACLA

Accession

Primary (citable) accession number: Q02147
Secondary accession number(s): Q9CG95

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	May 15, 2002
Last modified:	January 25, 2012
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program