ID   MROQ_STAA3              Reviewed;         247 AA.
AC   A0A0H2XEK8;
DT   05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=Membrane-embedded CAAX protease MroQ;
DE            EC=3.4.-.- {ECO:0000269|PubMed:30833334};
DE   Flags: Precursor;
GN   Name=MroQ;
OS   Staphylococcus aureus (strain USA300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=367830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300;
RX   PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA   Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA   Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA   Perdreau-Remington F.;
RT   "Complete genome sequence of USA300, an epidemic clone of community-
RT   acquired meticillin-resistant Staphylococcus aureus.";
RL   Lancet 367:731-739(2006).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-141; GLU-142 AND
RP   HIS-180.
RX   PubMed=30833334; DOI=10.1128/iai.00019-19;
RA   Cosgriff C.J., White C.R., Teoh W.P., Grayczyk J.P., Alonzo F. III;
RT   "Control of Staphylococcus aureus quorum sensing by a membrane-embedded
RT   peptidase.";
RL   Infect. Immun. 0:0-0(2019).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-141 AND GLU-142.
RX   PubMed=30833335; DOI=10.1128/iai.00002-19;
RA   Marroquin S., Gimza B., Tomlinson B., Stein M., Frey A., Keogh R.A.,
RA   Zapf R., Todd D.A., Cech N.B., Carroll R.K., Shaw L.N.;
RT   "MroQ is a novel Abi-domain protein that influences virulence gene
RT   expression in Staphylococcus aureus via modulation of Agr qctivity.";
RL   Infect. Immun. 0:0-0(2019).
CC   -!- FUNCTION: Participates in the regulation of the Agr quorum sensing
CC       activity and plays thereby an important role in virulence
CC       (PubMed:30833335, PubMed:30833334). Mechanistically, elicits a protease
CC       dependent control of Agr activity without playing a role in the
CC       processing of the pheromone-precursor AgrD (PubMed:30833335).
CC       {ECO:0000269|PubMed:30833334, ECO:0000269|PubMed:30833335}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Deletion results in decreased expression and
CC       abundance of secreted proteases, hemolysins and toxins, as well
CC       increased production of surface associated proteins (PubMed:30833334).
CC       A subsequent drastic reduction in proteolysis, hemolysis and
CC       pigmentation is observed (PubMed:30833335). In turn, virulence is
CC       attenuated (PubMed:30833334, PubMed:30833335).
CC       {ECO:0000269|PubMed:30833334, ECO:0000269|PubMed:30833335}.
CC   -!- SIMILARITY: Belongs to the peptidase U48 family. {ECO:0000305}.
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DR   EMBL; CP000255; ABD20720.1; -; Genomic_DNA.
DR   RefSeq; WP_000197635.1; NZ_CP027476.1.
DR   AlphaFoldDB; A0A0H2XEK8; -.
DR   SMR; A0A0H2XEK8; -.
DR   EnsemblBacteria; ABD20720; ABD20720; SAUSA300_1984.
DR   KEGG; saa:SAUSA300_1984; -.
DR   HOGENOM; CLU_079560_0_0_9; -.
DR   OMA; QMPIFIV; -.
DR   Proteomes; UP000001939; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0071586; P:CAAX-box protein processing; IEA:InterPro.
DR   InterPro; IPR003675; Rce1-like.
DR   Pfam; PF02517; Rce1-like; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Membrane; Protease; Signal; Transmembrane; Transmembrane helix;
KW   Virulence.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..247
FT                   /note="Membrane-embedded CAAX protease MroQ"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000447406"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        141
FT                   /evidence="ECO:0000305|PubMed:30833334"
FT   MUTAGEN         141
FT                   /note="E->A: About 90% loss of hemolytic activity."
FT                   /evidence="ECO:0000269|PubMed:30833334"
FT   MUTAGEN         141
FT                   /note="E->A: Complete loss of proteolytic and hemolytic
FT                   activity; in association with A-142."
FT                   /evidence="ECO:0000269|PubMed:30833335"
FT   MUTAGEN         142
FT                   /note="E->A: About 50% loss of hemolytic activity."
FT                   /evidence="ECO:0000269|PubMed:30833334"
FT   MUTAGEN         142
FT                   /note="E->A: Complete loss of proteolytic and hemolytic
FT                   activity; in association with A-141."
FT                   /evidence="ECO:0000269|PubMed:30833335"
FT   MUTAGEN         180
FT                   /note="H->A: About 90% loss of hemolytic activity."
FT                   /evidence="ECO:0000269|PubMed:30833334"
SQ   SEQUENCE   247 AA;  28163 MW;  F543A1DE5CDBEBDE CRC64;
     MTRLWASLLT VIIYILSQFL PLLIVKKLPF VQYSGIELTK AVIYIQLVLF LIAATTIILI
     NLKIKNPTKL ELEVKEPKKY IIPWALLGFA LVMIYQMVVS IVLTQIYGGQ QVSPNTEKLI
     IIARKIPIFI FFVSIIGPLL EEYVFRKVIF GELFNAIKGN RIVAFIIATT VSSLIFALAH
     NDFKFIPVYF GMGVIFSLAY VWTKRLAVPI IIHMLQNGFV VIFQLLNPEA LKKATEQANF
     IYHIFIP