ID   RNB_PROMH               Reviewed;         647 AA.
AC   B4EW02;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Exoribonuclease 2 {ECO:0000255|HAMAP-Rule:MF_01036};
DE            EC=3.1.13.1 {ECO:0000255|HAMAP-Rule:MF_01036};
DE   AltName: Full=Exoribonuclease II {ECO:0000255|HAMAP-Rule:MF_01036};
DE            Short=RNase II {ECO:0000255|HAMAP-Rule:MF_01036};
DE            Short=Ribonuclease II {ECO:0000255|HAMAP-Rule:MF_01036};
GN   Name=rnb {ECO:0000255|HAMAP-Rule:MF_01036}; OrderedLocusNames=PMI1311;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320;
RX   PubMed=18375554; DOI=10.1128/jb.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.T.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(2008).
CC   -!- FUNCTION: Involved in mRNA degradation. Hydrolyzes single-stranded
CC       polyribonucleotides processively in the 3' to 5' direction.
CC       {ECO:0000255|HAMAP-Rule:MF_01036}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC         nucleoside 5'-phosphates.; EC=3.1.13.1; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01036};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01036}.
CC   -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase II subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01036}.
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; AM942759; CAR42782.1; -; Genomic_DNA.
DR   RefSeq; WP_004243027.1; NC_010554.1.
DR   AlphaFoldDB; B4EW02; -.
DR   SMR; B4EW02; -.
DR   STRING; 529507.PMI1311; -.
DR   PRIDE; B4EW02; -.
DR   EnsemblBacteria; CAR42782; CAR42782; PMI1311.
DR   GeneID; 6801631; -.
DR   KEGG; pmr:PMI1311; -.
DR   eggNOG; COG4776; Bacteria.
DR   HOGENOM; CLU_002333_7_3_6; -.
DR   OMA; CFTNYLP; -.
DR   Proteomes; UP000008319; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:UniProt.
DR   GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.50.140; -; 2.
DR   HAMAP; MF_01036; RNase_II; 1.
DR   InterPro; IPR011129; CSD.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR013223; RNase_B_OB_dom.
DR   InterPro; IPR011804; RNase_II.
DR   InterPro; IPR001900; RNase_II/R.
DR   InterPro; IPR022966; RNase_II/R_CS.
DR   InterPro; IPR004476; RNase_II/RNase_R.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   Pfam; PF08206; OB_RNB; 1.
DR   Pfam; PF00773; RNB; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00357; CSP; 1.
DR   SMART; SM00955; RNB; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; SSF50249; 4.
DR   TIGRFAMs; TIGR00358; 3_prime_RNase; 1.
DR   TIGRFAMs; TIGR02062; RNase_B; 1.
DR   PROSITE; PS01175; RIBONUCLEASE_II; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..647
FT                   /note="Exoribonuclease 2"
FT                   /id="PRO_1000135872"
FT   DOMAIN          565..647
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ   SEQUENCE   647 AA;  74044 MW;  1A8945D7EDE48B33 CRC64;
     MFQDNPLLAQ LKQQLHAQTP RVEGLVKGTD KGFGFLEVDG QKSYFIPPPQ MKKVMHGDRI
     IAAVHTNNDK ESAEPEELVE PFLTRFVGRV QKKEGDNRLW IIPDHPLLKD AIPCRPIKSL
     THPFADQDWA VAEMRRHPLK GDKHFQAELT DFITDKDDHF APWWVTLMRH QLERNAPEVD
     SETLTLHDDL PREDLTALSF VTIDSASTED MDDALYIRKE ENGQLSLYIA IADPTAYIQP
     NSELDTIAAQ RALTNYLPGF NIPMLPRELS DNLCSLRPNE KRPALVCQVG IMEDGALTDE
     IHFYSAWVES KAKLVYDNIS DWLEGEETQW APENEIVHEQ VMLLKEMSEK RHVWREQHAL
     VFKERPDYRF ILDDSGNVLD IVAEKRRTAN RIVEEAMITA NICAAKVLSR NLGFGIYNVH
     TGFDPLYIDQ VSQTLKEHGI ETNADELLTL EGFCRLRREL DNQPNQFLDS RIRRFQNFAE
     IKTEPGPHFG LGLEAYATWT SPIRKYSDIL NHRLLKAIIS KSAAEKPQDE DCVRIAERRR
     ANRMAERDVG DWLYARFLKP FAGTESTFNA EIIDITRGGI RVRLVENGAI AFIPAPFLHA
     VRDEIQCSQE TGSVIIKGET AYKLNDIIPV RIEDVKLETR NIVARPI