ID   RNY_STAAN               Reviewed;         519 AA.
AC   P67278; Q99UI7;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 114.
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};
DE   AltName: Full=Conserved virulence factor A;
GN   Name=rny {ECO:0000255|HAMAP-Rule:MF_00335}; Synonyms=cvfA;
GN   OrderedLocusNames=SA1129;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=N315;
RA   Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT   "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT   aureus strain N315.";
RL   Submitted (OCT-2007) to UniProtKB.
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=20713508; DOI=10.1101/gad.1945010;
RA   Lopez D., Kolter R.;
RT   "Functional microdomains in bacterial membranes.";
RL   Genes Dev. 24:1893-1902(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       ECO:0000269|PubMed:20713508}; Single-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_00335}. Membrane raft
CC       {ECO:0000269|PubMed:20713508}; Single-pass membrane protein
CC       {ECO:0000255}. Note=Present in detergent-resistant membrane (DRM)
CC       fractions that may be equivalent to eukaryotic membrane rafts; these
CC       rafts include proteins involved in signaling, molecule trafficking and
CC       protein secretion. {ECO:0000269|PubMed:20713508}.
CC   -!- SIMILARITY: Belongs to the RNase Y family. {ECO:0000255|HAMAP-
CC       Rule:MF_00335}.
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DR   EMBL; BA000018; BAB42381.1; -; Genomic_DNA.
DR   PIR; A89903; A89903.
DR   RefSeq; WP_001050913.1; NC_002745.2.
DR   AlphaFoldDB; P67278; -.
DR   SMR; P67278; -.
DR   EnsemblBacteria; BAB42381; BAB42381; BAB42381.
DR   KEGG; sau:SA1129; -.
DR   HOGENOM; CLU_028328_1_0_9; -.
DR   OMA; PHAILGM; -.
DR   Proteomes; UP000000751; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
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   1: Evidence at protein level;
KW   Cell membrane; Endonuclease; Hydrolase; Membrane; Nuclease; RNA-binding;
KW   Transmembrane; Transmembrane helix; Virulence.
FT   CHAIN           1..519
FT                   /note="Ribonuclease Y"
FT                   /id="PRO_0000163788"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          209..269
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          335..428
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ   SEQUENCE   519 AA;  58512 MW;  076DE375A553FFA3 CRC64;
     MNLLSLLLIL LGIILGVVGG YVVARNLLLQ KQSQARQTAE DIVNQAHKEA DNIKKEKLLE
     AKEENQILRE QTEAELRERR SELQRQETRL LQKEENLERK SDLLDKKDEI LEQKESKIEE
     KQQQVDAKES SVQTLIMKHE QELERISGLT QEEAINEQLQ RVEEELSQDI AVLVKEKEKE
     AKEKVDKTAK ELLATAVQRL AADHTSESTV SVVNLPNDEM KGRIIGREGR NIRTLETLTG
     IDLIIDDTPE AVILSGFDPI RREIARTALV NLVSDGRIHP GRIEDMVEKA RKEVDDIIRE
     AGEQATFEVN AHNMHPDLVK IVGRLNYRTS YGQNVLKHSI EVAHLASMLA AELGEDETLA
     KRAGLLHDVG KAIDHEVEGS HVEIGVELAK KYGENETVIN AIHSHHGDVE PTSIISILVA
     AADALSAARP GARKETLENY IRRLERLETL SESYDGVEKA FAIQAGREIR VIVSPEEIDD
     LKSYRLARDI KNQIEDELQY PGHIKVTVVR ETRAVEYAK