RASP_BACLD
ID RASP_BACLD Reviewed; 419 AA.
AC Q65JJ2; Q62UZ7;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Zinc metalloprotease RasP;
DE EC=3.4.24.-;
DE AltName: Full=Regulating alternative sigma factor protease;
DE AltName: Full=Regulating anti-sigma-W factor activity protease;
GN Name=rasP; OrderedLocusNames=BLi01877, BL01236;
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15383718; DOI=10.1159/000079829;
RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT with great industrial potential.";
RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
CC -!- FUNCTION: Is responsible for Site-2 cleavage of the RsiW anti-sigma
CC factor. This results, after a third proteolytic step catalyzed by the
CC ClpXP protease, in the release of SigW and the transcription activation
CC of the genes under the control of the sigma-W factor (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR EMBL; AE017333; AAU40772.1; -; Genomic_DNA.
DR EMBL; CP000002; AAU23412.1; -; Genomic_DNA.
DR AlphaFoldDB; Q65JJ2; -.
DR SMR; Q65JJ2; -.
DR STRING; 279010.BL01236; -.
DR MEROPS; M50.011; -.
DR EnsemblBacteria; AAU23412; AAU23412; BL01236.
DR KEGG; bld:BLi01877; -.
DR KEGG; bli:BL01236; -.
DR PATRIC; fig|279010.13.peg.1876; -.
DR eggNOG; COG0750; Bacteria.
DR HOGENOM; CLU_025778_1_0_9; -.
DR OMA; QYMVGFG; -.
DR Proteomes; UP000000606; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR42837; PTHR42837; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR TIGRFAMs; TIGR00054; TIGR00054; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Cell membrane; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..419
FT /note="Zinc metalloprotease RasP"
FT /id="PRO_0000248826"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 184..269
FT /note="PDZ"
FT ACT_SITE 19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 419 AA; 46450 MW; 5AE47D9AD861C273 CRC64;
MNTVIAFILI FGTLVFFHEL GHLILAQRAG ILCREFAIGF GPKIFSFKKN ETVYTIRLLP
IGGFVRMAGE DPEMIEVKPG YTVGLLFDSE NKVEKIIINQ KEKYPDALVI EVEQADLEHQ
MRITGYEHGN EDHLSSFSVS ETSFFIVDGE EVQIAPYNRQ FHSKTVWQRI KAIAAGPIMN
FILAYVILVM LGLMQGVPSD EPVLGKLIDN GRAAEAGLQE GDRIQTINGE NMRSWTDIVN
TVREHPEKEL KIVLMRDNVK LTKYVTPEAV KAGDETVGRF GAYNPVKTGV LTSISYGATE
TATVAQSIVT NLGKLVTGQF SIDMLAGPVG IYDMTDQVAK TGVINLLKLA AFLSINLGIV
NLLPIPALDG GRLLFLFIEA IRGKPINREK EAFVVFIGVA FLMLLMLVVT WNDIQRLFL
