AARA_PROST
ID AARA_PROST Reviewed; 281 AA.
AC P46116;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Rhomboid protease AarA;
DE EC=3.4.21.105;
DE AltName: Full=Intramembrane serine protease;
GN Name=aarA;
OS Providencia stuartii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=588;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=PR50;
RX PubMed=8051030; DOI=10.1128/jb.176.16.5140-5144.1994;
RA Rather P.N., Orosz E.;
RT "Characterization of aarA, a pleiotrophic negative regulator of the 2'-N-
RT acetyltransferase in Providencia stuartii.";
RL J. Bacteriol. 176:5140-5144(1994).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15616571; DOI=10.1038/sj.emboj.7600537;
RA Lemberg M.K., Menendez J., Misik A., Garcia M., Koth C.M., Freeman M.;
RT "Mechanism of intramembrane proteolysis investigated with purified rhomboid
RT proteases.";
RL EMBO J. 24:464-472(2005).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-150.
RX PubMed=17215357; DOI=10.1073/pnas.0608140104;
RA Stevenson L.G., Strisovsky K., Clemmer K.M., Bhatt S., Freeman M.,
RA Rather P.N.;
RT "Rhomboid protease AarA mediates quorum-sensing in Providencia stuartii by
RT activating TatA of the twin-arginine translocase.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1003-1008(2007).
RN [4]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF ALA-149 AND SER-150.
RX PubMed=21439629; DOI=10.1016/j.cell.2011.02.047;
RA Zettl M., Adrain C., Strisovsky K., Lastun V., Freeman M.;
RT "Rhomboid family pseudoproteases use the ER quality control machinery to
RT regulate intercellular signaling.";
RL Cell 145:79-91(2011).
CC -!- FUNCTION: Rhomboid serine protease that catalyzes intramembrane
CC proteolysis. Mediates quorum-sensing and the subsequent regulation of
CC target genes via activation of the Tat protein export system. Catalyzes
CC the proteolytic activation of TatA by removal of its N-terminal
CC extension. {ECO:0000269|PubMed:15616571, ECO:0000269|PubMed:17215357,
CC ECO:0000269|PubMed:8051030}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleaves type-1 transmembrane domains using a catalytic dyad
CC composed of serine and histidine that are contributed by different
CC transmembrane domains.; EC=3.4.21.105;
CC Evidence={ECO:0000269|PubMed:21439629};
CC -!- INTERACTION:
CC P46116; A1YH68: tatA; NbExp=3; IntAct=EBI-10098058, EBI-10098044;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15616571,
CC ECO:0000269|PubMed:17215357}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15616571, ECO:0000269|PubMed:17215357}.
CC -!- MISCELLANEOUS: AarA deletion mutations display alterations in cell
CC morphology and total or partial loss of yellow pigmentation.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
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DR EMBL; L28755; AAA61597.1; -; Genomic_DNA.
DR PIR; A55862; A55862.
DR RefSeq; WP_004917931.1; NZ_WLUO01000038.1.
DR AlphaFoldDB; P46116; -.
DR SMR; P46116; -.
DR DIP; DIP-60798N; -.
DR IntAct; P46116; 2.
DR MINT; P46116; -.
DR STRING; 588.BGK56_18970; -.
DR BindingDB; P46116; -.
DR MEROPS; S54.004; -.
DR OMA; NVGLFVW; -.
DR BRENDA; 3.4.21.105; 5058.
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:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1540.10; -; 1.
DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR Pfam; PF01694; Rhomboid; 1.
DR SUPFAM; SSF144091; SSF144091; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Hydrolase; Membrane; Protease; Serine protease;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..281
FT /note="Rhomboid protease AarA"
FT /id="PRO_0000064416"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 150
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT ACT_SITE 210
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MUTAGEN 149
FT /note="A->P: Loss of proteolytic activity."
FT /evidence="ECO:0000269|PubMed:21439629"
FT MUTAGEN 150
FT /note="S->A: Loss of proteolytic activity."
FT /evidence="ECO:0000269|PubMed:17215357,
FT ECO:0000269|PubMed:21439629"
SQ SEQUENCE 281 AA; 31106 MW; 13EC8B5C66284B1E CRC64;
MAEQQNPFSI KSKARFSLGA IALTLTLVLL NIAVYFYQIV FASPLDSRES NLILFGANIY
QLSLTGDWWR YPISMMLHSN GTHLAFNCLA LFVIGIGCER AYGKFKLLAI YIISGIGAAL
FSAYWQYYEI SNSDLWTDST VYITIGVGAS GAIMGIAAAS VIYLIKVVIN KPNPHPVIQR
RQKYQLYNLI AMIALTLING LQSGVDNAAH IGGAIIGALI SIAYILVPHK LRVANLCITV
IAASLLTMMI YLYSFSTNKH LLEEREFIYQ EVYTELADAN Q
