ID   RASP_OCEIH              Reviewed;         424 AA.
AC   Q8EQU7;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 113.
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=OB1592;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC13548.1; -; Genomic_DNA.
DR   RefSeq; WP_011065992.1; NC_004193.1.
DR   AlphaFoldDB; Q8EQU7; -.
DR   SMR; Q8EQU7; -.
DR   STRING; 221109.22777275; -.
DR   MEROPS; M50.011; -.
DR   EnsemblBacteria; BAC13548; BAC13548; BAC13548.
DR   KEGG; oih:OB1592; -.
DR   eggNOG; COG0750; Bacteria.
DR   HOGENOM; CLU_025778_1_0_9; -.
DR   OMA; QYMVGFG; -.
DR   OrthoDB; 1395197at2; -.
DR   PhylomeDB; Q8EQU7; -.
DR   Proteomes; UP000000822; 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..424
FT                   /note="Zinc metalloprotease RasP"
FT                   /id="PRO_0000248828"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        317..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        351..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        396..416
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   424 AA;  47041 MW;  F054B135780EB742 CRC64;
     MTTVVAFILM FGVLVSIHEW GHLIFAKRAG MLVREFAIGF GPKIFSFTKN ETLYTIRLIP
     AGGYVRVAGE DPEIIELKPG HHIGLEFNQA GEVSKIIVNN KSKHPYARVI EVENVDLDHK
     LIIEGYELDD DENRLSFNVN EKAMFVMDER ETQIAPYNRQ FASKSTGKRA MQLFAGPMMN
     FVLAIAIFLI LGIIQGVPVE EAKLGEIQPD TPAEQAGFQQ DDVITQIGDQ SISTWEEFTS
     IVRENPGQEL DMVIQRNGES QDISVVPGEA EAVNEVGDPI TIGQIGVYQG FEKDVLGTFV
     YGIERTYDTT TMIIQNLFML VTGQVSIELL SGPVGIYDAT DQVVQTGFSN FLLWTAMLSI
     NLGIINLVPL PALDGGRLLF VGLEAVRGKP IAPEKEGIFH FVGFALLMLL MIVVTWNDIQ
     RLFL