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Protein

ATP phosphoribosyltransferase regulatory subunit

Gene

hisZ

Organism
Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.

Pathwayi: L-histidine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase (hisG), ATP phosphoribosyltransferase regulatory subunit (hisZ)
  2. Histidine biosynthesis bifunctional protein HisIE (hisI)
  3. Histidine biosynthesis bifunctional protein HisIE (hisI)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
  5. Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. Histidinol-phosphatase (hisK)
  9. Histidinol dehydrogenase (hisD)
This subpathway is part of the pathway L-histidine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Enzyme and pathway databases

BioCyciLLAC272623:GHSH-1294-MONOMER.
UniPathwayiUPA00031; UER00006.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP phosphoribosyltransferase regulatory subunit
Gene namesi
Name:hisZ
Ordered Locus Names:LL1207
ORF Names:L0341
OrganismiLactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
Taxonomic identifieri272623 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus
Proteomesi
  • UP000002196 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 328328ATP phosphoribosyltransferase regulatory subunitPRO_0000171038Add
BLAST

Proteomic databases

PaxDbiQ02147.

Interactioni

Subunit structurei

Heterooctamer composed of four HisG and four HisZ subunits.1 Publication

Protein-protein interaction databases

STRINGi272623.L0341.

Structurei

Secondary structure

1
328
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 123Combined sources
Helixi17 – 3620Combined sources
Beta strandi46 – 494Combined sources
Helixi50 – 578Combined sources
Beta strandi59 – 613Combined sources
Beta strandi70 – 723Combined sources
Beta strandi74 – 763Combined sources
Beta strandi78 – 814Combined sources
Helixi86 – 949Combined sources
Beta strandi102 – 1098Combined sources
Beta strandi116 – 1194Combined sources
Beta strandi125 – 13410Combined sources
Helixi136 – 15419Combined sources
Beta strandi157 – 1659Combined sources
Helixi166 – 17510Combined sources
Turni176 – 1783Combined sources
Helixi180 – 1889Combined sources
Helixi192 – 1998Combined sources
Helixi206 – 21510Combined sources
Helixi221 – 23010Combined sources
Helixi234 – 25017Combined sources
Turni251 – 2533Combined sources
Beta strandi256 – 2583Combined sources
Beta strandi271 – 2788Combined sources
Beta strandi281 – 29010Combined sources
Helixi292 – 2965Combined sources
Beta strandi298 – 3003Combined sources
Beta strandi305 – 3106Combined sources
Helixi311 – 32212Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z7MX-ray2.90A/B/C/D1-328[»]
1Z7NX-ray3.25A/B/C/D1-328[»]
ProteinModelPortaliQ02147.
SMRiQ02147. Positions 6-323.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02147.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108IQ6. Bacteria.
COG3705. LUCA.
HOGENOMiHOG000112907.
KOiK02502.
OrthoDBiEOG6BPDH4.

Family and domain databases

HAMAPiMF_00125. HisZ.
InterProiIPR006195. aa-tRNA-synth_II.
IPR004516. HisRS/HisZ.
IPR004517. HisZ.
[Graphical view]
PANTHERiPTHR11476. PTHR11476. 1 hit.
PIRSFiPIRSF001549. His-tRNA_synth. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q02147-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKINYLLPE ESAEMTLNQV KSLRQIEGRL RKLFSLKNYQ EVMPPSFEYT
60 70 80 90 100
QLYTALESNG KTFNQEKMFQ FIKHEGQSIT LRYDFTLPLV RLYSQIKDST
110 120 130 140 150
SARYSYFGKI FRKEKRHKGR STENYQIGIE LFGESADKSE LEILSLALQV
160 170 180 190 200
IEQLGLNKTV FEIGSAKFFQ RLCQLADGST ELLTELLLKK DLSGLNAFIE
210 220 230 240 250
KNNFSKELRG LLKEIFITNE LSRLENLVTN TKDDVLISSF DQLKEFSEKL
260 270 280 290 300
SMIKPIIIDL GMVPKMDYYT DLMFKAYSSA ANQPILSGGR YDQLLSNFQE
310 320
EAFAIGFCCH MDTILKALER QELEEDND
Length:328
Mass (Da):37,943
Last modified:May 15, 2002 - v2
Checksum:i2B47DC880331580D
GO

Sequence cautioni

The sequence AAK05305.1 differs from that shown. Reason: Frameshift at position 38. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731K → N in AAB81902 (PubMed:1400209).Curated
Sequence conflicti174 – 1741Q → H in AAB81902 (PubMed:1400209).Curated
Sequence conflicti210 – 2101G → E in AAB81902 (PubMed:1400209).Curated
Sequence conflicti303 – 3031F → V in AAB81902 (PubMed:1400209).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U92974 Genomic DNA. Translation: AAB81902.1.
AE005176 Genomic DNA. Translation: AAK05305.1. Frameshift.
PIRiC45734.
G86775.
RefSeqiNP_267363.1. NC_002662.1.

Genome annotation databases

EnsemblBacteriaiAAK05305; AAK05305; L0341.
GeneIDi1114854.
KEGGilla:L0341.
PATRICi22294788. VBILacLac136773_1302.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U92974 Genomic DNA. Translation: AAB81902.1.
AE005176 Genomic DNA. Translation: AAK05305.1. Frameshift.
PIRiC45734.
G86775.
RefSeqiNP_267363.1. NC_002662.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z7MX-ray2.90A/B/C/D1-328[»]
1Z7NX-ray3.25A/B/C/D1-328[»]
ProteinModelPortaliQ02147.
SMRiQ02147. Positions 6-323.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272623.L0341.

Proteomic databases

PaxDbiQ02147.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK05305; AAK05305; L0341.
GeneIDi1114854.
KEGGilla:L0341.
PATRICi22294788. VBILacLac136773_1302.

Phylogenomic databases

eggNOGiENOG4108IQ6. Bacteria.
COG3705. LUCA.
HOGENOMiHOG000112907.
KOiK02502.
OrthoDBiEOG6BPDH4.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00006.
BioCyciLLAC272623:GHSH-1294-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ02147.

Family and domain databases

HAMAPiMF_00125. HisZ.
InterProiIPR006195. aa-tRNA-synth_II.
IPR004516. HisRS/HisZ.
IPR004517. HisZ.
[Graphical view]
PANTHERiPTHR11476. PTHR11476. 1 hit.
PIRSFiPIRSF001549. His-tRNA_synth. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Histidine biosynthesis genes in Lactococcus lactis subsp. lactis."
    Delorme C., Ehrlich S.D., Renault P.
    J. Bacteriol. 174:6571-6579(1992) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.

Entry informationi

Entry nameiHISZ_LACLA
AccessioniPrimary (citable) accession number: Q02147
Secondary accession number(s): Q9CG95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: May 15, 2002
Last modified: November 11, 2015
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

This function is generally fulfilled by the C-terminal part of HisG, which is missing in some bacteria such as this one.
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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.