HISZ_LACLA
ID HISZ_LACLA Reviewed; 328 AA.
AC Q02147; Q9CG95;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2002, sequence version 2.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit;
GN Name=hisZ; OrderedLocusNames=LL1207; ORFNames=L0341;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCDO 2118;
RX PubMed=1400209; DOI=10.1128/jb.174.20.6571-6579.1992;
RA Delorme C., Ehrlich S.D., Renault P.;
RT "Histidine biosynthesis genes in Lactococcus lactis subsp. lactis.";
RL J. Bacteriol. 174:6571-6579(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
RN [3]
RP CHARACTERIZATION.
RX PubMed=10430882; DOI=10.1073/pnas.96.16.8985;
RA Sissler M., Delorme C., Bond J., Ehrlich S.D., Renault P., Francklyn C.;
RT "An aminoacyl-tRNA synthetase paralog with a catalytic role in histidine
RT biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:8985-8990(1999).
RN [4]
RP SUBUNIT.
RX PubMed=12269828; DOI=10.1021/bi020243z;
RA Bovee M.L., Champagne K.S., Demeler B., Francklyn C.S.;
RT "The quaternary structure of the HisZ-HisG N-1-(5'-phosphoribosyl)-ATP
RT transferase from Lactococcus lactis.";
RL Biochemistry 41:11838-11846(2002).
CC -!- FUNCTION: Required for the first step of histidine biosynthesis. May
CC allow the feedback regulation of ATP phosphoribosyltransferase activity
CC by histidine.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC -!- SUBUNIT: Heterooctamer composed of four HisG and four HisZ subunits.
CC {ECO:0000305|PubMed:12269828}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: This function is generally fulfilled by the C-terminal
CC part of HisG, which is missing in some bacteria such as this one.
CC -!- MISCELLANEOUS: The stability and homogeneity of the HisG-HisZ complex
CC is apparently increased by ATP and 5-phosphoribose 1-diphosphate but
CC decreased in the presence of the regulatory inhibitor histidine.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC HisZ subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK05305.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U92974; AAB81902.1; -; Genomic_DNA.
DR EMBL; AE005176; AAK05305.1; ALT_FRAME; Genomic_DNA.
DR PIR; C45734; C45734.
DR PIR; G86775; G86775.
DR RefSeq; NP_267363.1; NC_002662.1.
DR PDB; 1Z7M; X-ray; 2.90 A; A/B/C/D=1-328.
DR PDB; 1Z7N; X-ray; 3.25 A; A/B/C/D=1-328.
DR PDBsum; 1Z7M; -.
DR PDBsum; 1Z7N; -.
DR AlphaFoldDB; Q02147; -.
DR SMR; Q02147; -.
DR STRING; 272623.L0341; -.
DR PaxDb; Q02147; -.
DR EnsemblBacteria; AAK05305; AAK05305; L0341.
DR KEGG; lla:L0341; -.
DR PATRIC; fig|272623.7.peg.1302; -.
DR eggNOG; COG3705; Bacteria.
DR HOGENOM; CLU_025113_0_0_9; -.
DR UniPathway; UPA00031; UER00006.
DR EvolutionaryTrace; Q02147; -.
DR Proteomes; UP000002196; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00773; HisRS-like_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00125; HisZ; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR004516; HisRS/HisZ.
DR InterPro; IPR004517; HisZ.
DR PANTHER; PTHR43707; PTHR43707; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW Reference proteome.
FT CHAIN 1..328
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_0000171038"
FT CONFLICT 73
FT /note="K -> N (in Ref. 1; AAB81902)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="Q -> H (in Ref. 1; AAB81902)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="G -> E (in Ref. 1; AAB81902)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="F -> V (in Ref. 1; AAB81902)"
FT /evidence="ECO:0000305"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:1Z7N"
FT HELIX 17..36
FT /evidence="ECO:0007829|PDB:1Z7M"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:1Z7M"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:1Z7M"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:1Z7M"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1Z7M"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1Z7N"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1Z7M"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:1Z7M"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:1Z7M"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:1Z7M"
FT STRAND 125..134
FT /evidence="ECO:0007829|PDB:1Z7M"
FT HELIX 136..154
FT /evidence="ECO:0007829|PDB:1Z7M"
FT STRAND 157..165
FT /evidence="ECO:0007829|PDB:1Z7M"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:1Z7M"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:1Z7M"
FT HELIX 180..188
FT /evidence="ECO:0007829|PDB:1Z7M"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:1Z7M"
FT HELIX 206..215
FT /evidence="ECO:0007829|PDB:1Z7M"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:1Z7M"
FT HELIX 234..250
FT /evidence="ECO:0007829|PDB:1Z7M"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:1Z7M"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:1Z7N"
FT STRAND 271..278
FT /evidence="ECO:0007829|PDB:1Z7M"
FT STRAND 281..290
FT /evidence="ECO:0007829|PDB:1Z7M"
FT HELIX 292..296
FT /evidence="ECO:0007829|PDB:1Z7M"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:1Z7M"
FT STRAND 305..310
FT /evidence="ECO:0007829|PDB:1Z7M"
FT HELIX 311..322
FT /evidence="ECO:0007829|PDB:1Z7M"
SQ SEQUENCE 328 AA; 37943 MW; 2B47DC880331580D CRC64;
MEKINYLLPE ESAEMTLNQV KSLRQIEGRL RKLFSLKNYQ EVMPPSFEYT QLYTALESNG
KTFNQEKMFQ FIKHEGQSIT LRYDFTLPLV RLYSQIKDST SARYSYFGKI FRKEKRHKGR
STENYQIGIE LFGESADKSE LEILSLALQV IEQLGLNKTV FEIGSAKFFQ RLCQLADGST
ELLTELLLKK DLSGLNAFIE KNNFSKELRG LLKEIFITNE LSRLENLVTN TKDDVLISSF
DQLKEFSEKL SMIKPIIIDL GMVPKMDYYT DLMFKAYSSA ANQPILSGGR YDQLLSNFQE
EAFAIGFCCH MDTILKALER QELEEDND
