YBEY_HAEIN
ID YBEY_HAEIN Reviewed; 154 AA.
AC P71335;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Endoribonuclease YbeY {ECO:0000255|HAMAP-Rule:MF_00009};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00009};
GN Name=ybeY {ECO:0000255|HAMAP-Rule:MF_00009}; OrderedLocusNames=HI_0004;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP STRUCTURE BY NMR, COFACTOR, AND ZINC BINDING.
RX PubMed=15632286; DOI=10.1110/ps.041096705;
RA Yeh D.C., Parsons L.M., Parsons J.F., Liu F., Eisenstein E., Orban J.;
RT "NMR structure of HI0004, a putative essential gene product from
RT Haemophilus influenzae, and comparison with the X-ray structure of an
RT Aquifex aeolicus homolog.";
RL Protein Sci. 14:424-430(2005).
CC -!- FUNCTION: Single strand-specific metallo-endoribonuclease involved in
CC late-stage 70S ribosome quality control and in maturation of the 3'
CC terminus of the 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00009}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00009,
CC ECO:0000269|PubMed:15632286};
CC Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_00009,
CC ECO:0000269|PubMed:15632286};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00009}.
CC -!- SIMILARITY: Belongs to the endoribonuclease YbeY family.
CC {ECO:0000255|HAMAP-Rule:MF_00009}.
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; L42023; AAC21683.1; -; Genomic_DNA.
DR PIR; A64140; A64140.
DR RefSeq; NP_438177.1; NC_000907.1.
DR RefSeq; WP_005663323.1; NC_000907.1.
DR PDB; 1XAX; NMR; -; A=1-154.
DR PDBsum; 1XAX; -.
DR AlphaFoldDB; P71335; -.
DR BMRB; P71335; -.
DR SMR; P71335; -.
DR STRING; 71421.HI_0004; -.
DR EnsemblBacteria; AAC21683; AAC21683; HI_0004.
DR KEGG; hin:HI_0004; -.
DR PATRIC; fig|71421.8.peg.4; -.
DR eggNOG; COG0319; Bacteria.
DR HOGENOM; CLU_106710_0_1_6; -.
DR OMA; RMRIHPL; -.
DR PhylomeDB; P71335; -.
DR BioCyc; HINF71421:G1GJ1-4-MON; -.
DR EvolutionaryTrace; P71335; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004521; F:endoribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.390.30; -; 1.
DR HAMAP; MF_00009; Endoribonucl_YbeY; 1.
DR InterPro; IPR023091; MetalPrtase_cat_dom_sf_prd.
DR InterPro; IPR002036; YbeY.
DR InterPro; IPR020549; YbeY_CS.
DR PANTHER; PTHR46986; PTHR46986; 1.
DR Pfam; PF02130; YbeY; 1.
DR TIGRFAMs; TIGR00043; TIGR00043; 1.
DR PROSITE; PS01306; UPF0054; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW Reference proteome; Ribosome biogenesis; rRNA processing; Zinc.
FT CHAIN 1..154
FT /note="Endoribonuclease YbeY"
FT /id="PRO_0000102463"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00009,
FT ECO:0000269|PubMed:15632286"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00009,
FT ECO:0000269|PubMed:15632286"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00009,
FT ECO:0000269|PubMed:15632286"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:1XAX"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:1XAX"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1XAX"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:1XAX"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:1XAX"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:1XAX"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:1XAX"
FT HELIX 90..100
FT /evidence="ECO:0007829|PDB:1XAX"
FT HELIX 104..117
FT /evidence="ECO:0007829|PDB:1XAX"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:1XAX"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:1XAX"
FT HELIX 129..141
FT /evidence="ECO:0007829|PDB:1XAX"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:1XAX"
SQ SEQUENCE 154 AA; 17355 MW; C066F7AB7F9CA7AD CRC64;
MGSVLVDLQI ATENIEGLPT EEQIVQWATG AVQPEGNEVE MTVRIVDEAE SHELNLTYRG
KDRPTNVLSF PFECPDEVEL PLLGDLVICR QVVEREASEQ EKPLMAHWAH MVVHGSLHLL
GYDHIEDDEA EEMESLETQI MQGLGFDDPY LAEK
