Y5695_STRCO
ID Y5695_STRCO Reviewed; 430 AA.
AC Q9KYS0;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Putative zinc metalloprotease SCO5695;
DE EC=3.4.24.-;
GN OrderedLocusNames=SCO5695; ORFNames=SC5H4.19;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
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; AL939124; CAB91131.1; -; Genomic_DNA.
DR RefSeq; NP_629823.1; NC_003888.3.
DR RefSeq; WP_011030397.1; NZ_VNID01000024.1.
DR AlphaFoldDB; Q9KYS0; -.
DR STRING; 100226.SCO5695; -.
DR GeneID; 1101134; -.
DR KEGG; sco:SCO5695; -.
DR PATRIC; fig|100226.15.peg.5784; -.
DR eggNOG; COG0750; Bacteria.
DR HOGENOM; CLU_025778_1_2_11; -.
DR InParanoid; Q9KYS0; -.
DR OMA; QYMVGFG; -.
DR PhylomeDB; Q9KYS0; -.
DR Proteomes; UP000001973; 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 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..430
FT /note="Putative zinc metalloprotease SCO5695"
FT /id="PRO_0000088465"
FT TRANSMEM 122..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 146..227
FT /note="PDZ"
FT ACT_SITE 21
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 430 AA; 46240 MW; 3586AEBD3FD1F44F CRC64;
MFILGIVLFA VGLLFSIAWH ELGHLSTAKM FGIRVPQYMV GFGPTLFSKK KGDTEYGVKA
IPFGGYIRMI GMFPPGPDGR MEARSTSPWR GMIEDARSAA FEELQPGDEK RLFYTRKPWK
RVIVMFAGPF MNLILAVVLF LTVLMGFGIS QQTTTVSSVS QCVISQSENP DDCAKSDPAS
PAAAAGLRAG DKILAFDGVR TDDWDKLSDL IRANPGEDVP VVVERKGEEI TLHATIATNK
VAKKDSNGQI VQGEYVTAGF LGFSSATGVV KQDFGQSVTW MGDRIGDAVD NLAALPAKIP
ALWDAAFGDG PREADSPMGV VGAARVGGEI ATLDIPPTQQ LAMFVMLVAG FNLSLFLFNM
LPLLPLDGGH IAGALWESLR RATAKVLRRP DPGPFDVAKL MPVAYVVAGV FVCFTLLVLV
ADVVNPVRIT