RNJ2_STAES
ID RNJ2_STAES Reviewed; 557 AA.
AC Q8CST0;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Ribonuclease J 2 {ECO:0000255|HAMAP-Rule:MF_01491};
DE Short=RNase J2 {ECO:0000255|HAMAP-Rule:MF_01491};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01491};
GN Name=rnj2 {ECO:0000255|HAMAP-Rule:MF_01491}; OrderedLocusNames=SE_0952;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
CC -!- FUNCTION: An RNase that has 5'-3' exonuclease and possibly
CC endoonuclease activity. Involved in maturation of rRNA and in some
CC organisms also mRNA maturation and/or decay (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01491};
CC Note=Binds up to 2 Zn(2+) ions per subunit. It is not clear if Zn(2+)
CC or Mg(2+) is physiologically important. {ECO:0000255|HAMAP-
CC Rule:MF_01491};
CC -!- SUBUNIT: Homodimer, may be a subunit of the RNA degradosome.
CC {ECO:0000255|HAMAP-Rule:MF_01491}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01491}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC metabolizing metallo-beta-lactamase-like family. Bacterial RNase J
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01491}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO04549.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE015929; AAO04549.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_764507.1; NC_004461.1.
DR RefSeq; WP_002457357.1; NZ_WBME01000001.1.
DR PDB; 6K6W; X-ray; 2.70 A; A/B/C/D=1-557.
DR PDBsum; 6K6W; -.
DR AlphaFoldDB; Q8CST0; -.
DR SMR; Q8CST0; -.
DR STRING; 176280.SE_0952; -.
DR EnsemblBacteria; AAO04549; AAO04549; SE_0952.
DR GeneID; 50018913; -.
DR KEGG; sep:SE_0952; -.
DR PATRIC; fig|176280.10.peg.926; -.
DR eggNOG; COG0595; Bacteria.
DR HOGENOM; CLU_008727_3_1_9; -.
DR Proteomes; UP000001411; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004534; F:5'-3' exoribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004521; F:endoribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.10710; -; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR HAMAP; MF_01491; RNase_J_bact; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR011108; RMMBL.
DR InterPro; IPR004613; RNase_J.
DR InterPro; IPR042173; RNase_J_2.
DR InterPro; IPR030854; RNase_J_bac.
DR InterPro; IPR041636; RNase_J_C.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF07521; RMMBL; 1.
DR Pfam; PF17770; RNase_J_C; 1.
DR PIRSF; PIRSF004803; RnjA; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR TIGRFAMs; TIGR00649; MG423; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endonuclease; Exonuclease; Hydrolase;
KW Metal-binding; Nuclease; RNA-binding; rRNA processing; Zinc.
FT CHAIN 1..557
FT /note="Ribonuclease J 2"
FT /id="PRO_0000286855"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 366..370
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT STRAND 11..22
FT /evidence="ECO:0007829|PDB:6K6W"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:6K6W"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:6K6W"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:6K6W"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:6K6W"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:6K6W"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:6K6W"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:6K6W"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:6K6W"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:6K6W"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6K6W"
FT HELIX 100..112
FT /evidence="ECO:0007829|PDB:6K6W"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:6K6W"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:6K6W"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:6K6W"
FT STRAND 145..156
FT /evidence="ECO:0007829|PDB:6K6W"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:6K6W"
FT HELIX 181..190
FT /evidence="ECO:0007829|PDB:6K6W"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:6K6W"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:6K6W"
FT HELIX 211..222
FT /evidence="ECO:0007829|PDB:6K6W"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:6K6W"
FT HELIX 238..250
FT /evidence="ECO:0007829|PDB:6K6W"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:6K6W"
FT HELIX 264..271
FT /evidence="ECO:0007829|PDB:6K6W"
FT HELIX 285..290
FT /evidence="ECO:0007829|PDB:6K6W"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:6K6W"
FT STRAND 296..305
FT /evidence="ECO:0007829|PDB:6K6W"
FT HELIX 306..315
FT /evidence="ECO:0007829|PDB:6K6W"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:6K6W"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:6K6W"
FT HELIX 341..353
FT /evidence="ECO:0007829|PDB:6K6W"
FT HELIX 373..383
FT /evidence="ECO:0007829|PDB:6K6W"
FT STRAND 385..393
FT /evidence="ECO:0007829|PDB:6K6W"
FT HELIX 395..408
FT /evidence="ECO:0007829|PDB:6K6W"
FT HELIX 412..414
FT /evidence="ECO:0007829|PDB:6K6W"
FT STRAND 422..426
FT /evidence="ECO:0007829|PDB:6K6W"
FT STRAND 431..436
FT /evidence="ECO:0007829|PDB:6K6W"
FT STRAND 441..444
FT /evidence="ECO:0007829|PDB:6K6W"
SQ SEQUENCE 557 AA; 62677 MW; 0A93CCC9657C3AF7 CRC64;
MSLIKKKNKD IRIIPLGGVG EIAKNMYIVE VDDEMFMLDA GLMFPEDEML GVDIVIPDIQ
YVIENKERLK GIFLTHGHEH AIGAVSYVLE QIDAPVYGSK LTIALVKEAM KARNIKKKVR
YYTVNHDSIM RFKNVNVSFF NTTHSIPDSL GVCIHTSYGS IVYTGEFKFD QSLHGHYAPD
LKRMAEIGDE GVFALISDST EAEKPGYNTP ENIIEHHMYD AFAKVKGRLI VSCYASNFVR
IQQVLNIASQ LNRKVSFLGR SLESSFNIAR KMGYFDIPKD LLIPINEVEN YPKNEVIIIA
TGMQGEPVEA LSQMARKKHK IMNIEEGDSI FLAITASANM EVIIADTLNE LVRAGAHIIP
NNKKIHASSH GCMEELKMML NIMKPEYFVP VQGEFKMQIA HAKLAAETGV APEKIFLVEK
GDVISYNGKD MILNEKVQSG NILIDGIGVG DVGNIVLRDR HLLAEDGIFI AVVTLDPKNR
RIAAGPEIQS RGFVYVRESE ELLKEAEEKV RKIVEEGLQE KRIEWSEIKQ NMRDQISKLL
FESTKRRPMI IPVISEI
