RNY_STAA1
ID RNY_STAA1 Reviewed; 519 AA.
AC A7X1S5;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 100.
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=SAHV_1276;
OS Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=418127;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu3 / ATCC 700698;
RX PubMed=17954695; DOI=10.1128/aac.00534-07;
RA Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT "Mutated response regulator graR is responsible for phenotypic conversion
RT of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT resistance to vancomycin-intermediate resistance.";
RL Antimicrob. Agents Chemother. 52:45-53(2008).
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; AP009324; BAF78159.1; -; Genomic_DNA.
DR RefSeq; WP_001050913.1; NC_009782.1.
DR AlphaFoldDB; A7X1S5; -.
DR SMR; A7X1S5; -.
DR KEGG; saw:SAHV_1276; -.
DR HOGENOM; CLU_028328_1_0_9; -.
DR OMA; PHAILGM; -.
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; Virulence.
FT CHAIN 1..519
FT /note="Ribonuclease Y"
FT /id="PRO_0000344934"
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