ID   RNY_STRPI               Reviewed;         537 AA.
AC   B1I7K2;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Ribonuclease Y {ECO:0000255|HAMAP-Rule:MF_00335};
DE            Short=RNase Y {ECO:0000255|HAMAP-Rule:MF_00335};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00335};
GN   Name=rny {ECO:0000255|HAMAP-Rule:MF_00335}; OrderedLocusNames=SPH_1848;
OS   Streptococcus pneumoniae (strain Hungary19A-6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=487214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hungary19A-6;
RX   PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA   Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA   Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA   Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA   Rappuoli R., Moxon E.R., Masignani V.;
RT   "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT   closely related species.";
RL   Genome Biol. 11:R107.1-R107.19(2010).
CC   -!- FUNCTION: Endoribonuclease that initiates mRNA decay.
CC       {ECO:0000255|HAMAP-Rule:MF_00335}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00335};
CC       Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00335}.
CC   -!- SIMILARITY: Belongs to the RNase Y family. {ECO:0000255|HAMAP-
CC       Rule:MF_00335}.
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DR   EMBL; CP000936; ACA37436.1; -; Genomic_DNA.
DR   RefSeq; WP_000404940.1; NC_010380.1.
DR   AlphaFoldDB; B1I7K2; -.
DR   SMR; B1I7K2; -.
DR   PRIDE; B1I7K2; -.
DR   EnsemblBacteria; ACA37436; ACA37436; SPH_1848.
DR   GeneID; 60232790; -.
DR   GeneID; 66806812; -.
DR   KEGG; spv:SPH_1848; -.
DR   HOGENOM; CLU_028328_1_0_9; -.
DR   OMA; PHAILGM; -.
DR   Proteomes; UP000002163; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004521; F:endoribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00077; HDc; 1.
DR   Gene3D; 3.30.1370.10; -; 1.
DR   HAMAP; MF_00335; RNase_Y; 1.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR006675; HDIG_dom.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR017705; Ribonuclease_Y.
DR   InterPro; IPR022711; RNase_Y_N.
DR   PANTHER; PTHR12826:SF15; PTHR12826:SF15; 1.
DR   Pfam; PF01966; HD; 1.
DR   Pfam; PF00013; KH_1; 1.
DR   Pfam; PF12072; RNase_Y_N; 1.
DR   SMART; SM00471; HDc; 1.
DR   SMART; SM00322; KH; 1.
DR   SUPFAM; SSF54791; SSF54791; 1.
DR   TIGRFAMs; TIGR00277; HDIG; 1.
DR   TIGRFAMs; TIGR03319; RNase_Y; 1.
DR   PROSITE; PS51831; HD; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Endonuclease; Hydrolase; Membrane; Nuclease; RNA-binding;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..537
FT                   /note="Ribonuclease Y"
FT                   /id="PRO_0000344941"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          227..290
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          353..446
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   REGION          114..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   537 AA;  60230 MW;  E1DDE3324BC3537C CRC64;
     MEIMSLAIAV FAVIIGLVIG YVSISAKMKS SQEAAELMLL NAEQEATNLR GQAEREADLL
     VNEAKRESKS LKKEALLEAK EEARKYREEV DAEFKSERQE LKQIESRLTE RATSLDRKDD
     NLTSKEQTLE QKEQSISDRA KNLDAREEQL EEVERQKEAE LERIGALSQA EARDIILAQT
     EENLTREIAS RIREAEQEVK ERSDKMAKDI LVQAMQRIAG EYVAESTNST VHLPDDTMKG
     RIIGREGRNI RTFESLTGVD VIIDDTPEVV TLSGFDPIRR EIARMTMEML LKDGRIHPAR
     IEELVEKNRQ EIDNKIREYG EAAAYEIGAP NLHPDLMKIM GRLQFRTSYG QNVLRHSIEV
     AKLAGIMASE LGENAALARR AGFLHDIGKA IDHEVEGSHV EIGMELARKY KEPPVVVNTI
     ASHHGDVEAE SVIAVIVAAA DALSAARPGA RSESLESYIK RLHDLEEIAN GFEGVQTSFA
     LQAGREIRIM VNPGKIKDDK VTILAHKVRK KIENNLDYPG NIKVTVIREL RAVDYAK