SYC_HELPY
ID SYC_HELPY Reviewed; 465 AA.
AC P41259;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Cysteine--tRNA ligase;
DE EC=6.1.1.16;
DE AltName: Full=Cysteinyl-tRNA synthetase;
DE Short=CysRS;
GN Name=cysS; OrderedLocusNames=HP_0886;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 278-465.
RC STRAIN=ATCC 49503 / 60190;
RX PubMed=8144644; DOI=10.1016/s0021-9258(17)34097-8;
RA Cover T.L., Tummuru M.K., Cao P., Thompson S.A., Blaser M.J.;
RT "Divergence of genetic sequences for the vacuolating cytotoxin among
RT Helicobacter pylori strains.";
RL J. Biol. Chem. 269:10566-10573(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 407-465.
RC STRAIN=DSM 4867 / CCUG 17874 / NCTC 11638;
RX PubMed=8168917; DOI=10.1128/iai.62.5.1557-1565.1994;
RA Phadnis S.H., Ilver D.J., Janzon L., Normark S., Westblom T.U.;
RT "Pathological significance and molecular characterization of the
RT vacuolating toxin gene of Helicobacter pylori.";
RL Infect. Immun. 62:1557-1565(1994).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-
CC cysteinyl-tRNA(Cys); Xref=Rhea:RHEA:17773, Rhea:RHEA-COMP:9661,
CC Rhea:RHEA-COMP:9679, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:78442, ChEBI:CHEBI:78517,
CC ChEBI:CHEBI:456215; EC=6.1.1.16;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {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; AE000511; AAD07934.1; -; Genomic_DNA.
DR EMBL; U05676; AAA17656.1; -; Unassigned_DNA.
DR EMBL; U07145; AAA18866.1; -; Unassigned_DNA.
DR PIR; F64630; F64630.
DR RefSeq; NP_207679.1; NC_000915.1.
DR RefSeq; WP_000471359.1; NC_018939.1.
DR AlphaFoldDB; P41259; -.
DR SMR; P41259; -.
DR DIP; DIP-3687N; -.
DR IntAct; P41259; 1.
DR MINT; P41259; -.
DR STRING; 85962.C694_04540; -.
DR PaxDb; P41259; -.
DR EnsemblBacteria; AAD07934; AAD07934; HP_0886.
DR KEGG; hpy:HP_0886; -.
DR PATRIC; fig|85962.47.peg.942; -.
DR eggNOG; COG0215; Bacteria.
DR OMA; AKYWMHN; -.
DR PhylomeDB; P41259; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0004817; F:cysteine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00672; CysRS_core; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00041; Cys_tRNA_synth; 1.
DR InterPro; IPR015803; Cys-tRNA-ligase.
DR InterPro; IPR015273; Cys-tRNA-synt_Ia_DALR.
DR InterPro; IPR024909; Cys-tRNA/MSH_ligase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR032678; tRNA-synt_1_cat_dom.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR PANTHER; PTHR10890; PTHR10890; 1.
DR Pfam; PF09190; DALR_2; 1.
DR Pfam; PF01406; tRNA-synt_1e; 1.
DR PRINTS; PR00983; TRNASYNTHCYS.
DR SMART; SM00840; DALR_2; 1.
DR SUPFAM; SSF47323; SSF47323; 1.
DR TIGRFAMs; TIGR00435; cysS; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..465
FT /note="Cysteine--tRNA ligase"
FT /id="PRO_0000159409"
FT MOTIF 29..39
FT /note="'HIGH' region"
FT MOTIF 269..273
FT /note="'KMSKS' region"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT VARIANT 280
FT /note="V -> I (in strain: ATCC 49503)"
FT VARIANT 332
FT /note="T -> N (in strain: ATCC 49503)"
FT VARIANT 392
FT /note="I -> V (in strain: ATCC 49503)"
FT VARIANT 432
FT /note="R -> Q (in strain: ATCC 49503 and NCTC 11638)"
FT VARIANT 434
FT /note="D -> N (in strain: NCTC 11638)"
FT VARIANT 440
FT /note="S -> H (in strain: ATCC 49503)"
SQ SEQUENCE 465 AA; 53132 MW; B7053D58BCD87F30 CRC64;
MFIYDTKLKQ KVPFEPLVQN KANIYVCGPT VYDDAHLGHA RSAIAFDLLR RTLELSGYEV
MLVRNFTDID DKIINKALKE NKSIQELSSI YIESYTRDLN ALNVKKPSLE PKASEYLDAM
VGMIETLLEK NIAYQVSNGD IYLDTSKDKD YGSLSVHNSS IEFGRIGLVQ EKRLEQDFVL
WKSYKGDNDV GFDSPLGKGR PGWHIECSSM VFETLALTNT PYQIDIHAGG ADLLFPHHEN
EACQTRCAFG VELAKYWMHN GFVNINNEKM SKSLGNSFFV KDALKNYDGE ILRNYLLGVH
YRSVLNFNEE DLLVSKKRLD KIYRLKQRVL GTLGGINPNF KKEILECMQD DLNVSKALSV
LESMLSSTNE KLDQNPKNKA LKGEILANLK FIEELLGIGF KDPSAYFQLG VSESEKQEIE
NKIEERKRAK ERKDFLKADS IREELLKQKI ALMDTPQGTI WEKFF
