ID S5V420_STRC3 Unreviewed; 688 AA.
AC S5V420;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Neutral zinc metalloprotease {ECO:0000313|EMBL:AGS69859.1};
GN ORFNames=B446_15205 {ECO:0000313|EMBL:AGS69859.1};
OS Streptomyces collinus (strain DSM 40733 / Tue 365).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1214242 {ECO:0000313|EMBL:AGS69859.1, ECO:0000313|Proteomes:UP000015423};
RN [1] {ECO:0000313|Proteomes:UP000015423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40733 / Tue 365 {ECO:0000313|Proteomes:UP000015423};
RA Ruckert C., Szczepanowski R., Goesmann A., Pross E.K., Musiol E.M.,
RA Blin K., Wohlleben W., Puhler A., Weber T., Kalinowski J.;
RT "The complete genome sequence of Streptomyces collinus Tu 365.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGS69859.1, ECO:0000313|Proteomes:UP000015423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40733 / Tue 365 {ECO:0000313|Proteomes:UP000015423};
RX PubMed=24140291; DOI=10.1016/j.jbiotec.2013.10.004;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Iftime D.,
RA Musiol E.M., Blin K., Wohlleben W., Puhler A., Kalinowski J., Weber T.;
RT "Complete genome sequence of the kirromycin producer Streptomyces collinus
RT Tu 365 consisting of a linear chromosome and two linear plasmids.";
RL J. Biotechnol. 168:739-740(2013).
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DR EMBL; CP006259; AGS69859.1; -; Genomic_DNA.
DR RefSeq; WP_020940330.1; NC_021985.1.
DR AlphaFoldDB; S5V420; -.
DR STRING; 1214242.B446_15205; -.
DR KEGG; sci:B446_15205; -.
DR PATRIC; fig|1214242.5.peg.3113; -.
DR eggNOG; COG4934; Bacteria.
DR HOGENOM; CLU_012501_0_0_11; -.
DR Proteomes; UP000015423; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04056; Peptidases_S53; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR030400; Sedolisin_dom.
DR PANTHER; PTHR14218:SF42; PEPTIDASE S53 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR Pfam; PF05345; He_PIG; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49313; Cadherin-like; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51695; SEDOLISIN; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:AGS69859.1};
KW Metalloprotease {ECO:0000313|EMBL:AGS69859.1};
KW Protease {ECO:0000313|EMBL:AGS69859.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015423};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..688
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038440727"
FT DOMAIN 115..447
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
SQ SEQUENCE 688 AA; 69326 MW; 7E9626D798C27B94 CRC64;
MRESRPSGRR RSLRRLVSIA LPALALTVAG LVAAPTAGAH TTAAHPHTGK ATQNAKALTD
PQRQIFHSTG KAGQKVPTTH LCATAAPGHA SCFAQRRTDI RQRLASALAA AAPSGLSPAN
LHSAYNLPTS GGSGLTVAVV DAYNDPNAES DLATYRSTYG LSACTKANGC FKQVSQTGST
TSLPTNDTGW AGEEALDLDM VSAVCPNCNI VLVEASSAND SDLGIAENEA VSLGAKFVSN
SWGGSESSTQ TSEDTQYFKH PGVAITVSSG DSAYGAEYPA TSQYVTAVGG TALSTASNSR
GWSESVWHTS STEGTGSGCS AYDPKPSWQT DASCSKRMEA DVSAVADPAT GVAVYDTYGG
SGWAVYGGTS ASAPIIAGVY ALAGTPASGD YPAKYPYAHT GNLYDVTSGS NGSCTTSYFC
TARTGYDGPT GWGTPNGTTA FTGGTSTGNT VTVTNPGSQS TTTGGSVSLQ IKASDSAGAA
LTYSASGLPT GLSVNSTSGL ISGTASTAGT YQVTVTATDS TGASGATSFT WTVGGSGGTC
TSAQLLANPG FESGSTGWTS STGVITTDTG EAAHGGSYKA WLDGYGSAHT DTLSQSVTVP
SGCKATFTFY LHVDTAETGS TAYDKLTVSA GSTTLATYSN VNAASGYTQK TFDLSSFAGQ
TVTLKFSGVE DSSLQTSFVV DDTALTTG
//
