ID V6KWE2_STRRC Unreviewed; 688 AA.
AC V6KWE2;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN ORFNames=M878_13260 {ECO:0000313|EMBL:EST33299.1};
OS Streptomyces roseochromogenus subsp. oscitans DS 12.976.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1352936 {ECO:0000313|EMBL:EST33299.1, ECO:0000313|Proteomes:UP000017984};
RN [1] {ECO:0000313|EMBL:EST33299.1, ECO:0000313|Proteomes:UP000017984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS 12.976 {ECO:0000313|EMBL:EST33299.1,
RC ECO:0000313|Proteomes:UP000017984};
RX PubMed=24407645;
RA Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT "Draft Genome Sequence of Streptomyces roseochromogenes subsp. oscitans DS
RT 12.976, Producer of the Aminocoumarin Antibiotic Clorobiocin.";
RL Genome Announc. 2:e01147-e01113(2014).
CC -!- FUNCTION: Extracellular zinc metalloprotease.
CC {ECO:0000256|RuleBase:RU366073}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU366073};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU366073}.
CC -!- SIMILARITY: Belongs to the peptidase M4 family.
CC {ECO:0000256|ARBA:ARBA00009388, ECO:0000256|RuleBase:RU366073}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EST33299.1}.
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DR EMBL; AWQX01000110; EST33299.1; -; Genomic_DNA.
DR RefSeq; WP_023546657.1; NZ_CM002285.1.
DR AlphaFoldDB; V6KWE2; -.
DR STRING; 1352936.M878_13260; -.
DR MEROPS; M04.017; -.
DR PATRIC; fig|1352936.5.peg.2796; -.
DR HOGENOM; CLU_008590_5_1_11; -.
DR OrthoDB; 291295at2; -.
DR Proteomes; UP000017984; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09597; M4_TLP; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 3.10.450.40; -; 1.
DR Gene3D; 3.10.450.490; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR PANTHER; PTHR33794:SF1; BACILLOLYSIN; 1.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366073};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU366073};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366073};
KW Reference proteome {ECO:0000313|Proteomes:UP000017984};
KW Secreted {ECO:0000256|RuleBase:RU366073};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU366073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT SIGNAL 1..51
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT CHAIN 52..688
FT /note="Neutral metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT /id="PRO_5023144352"
FT DOMAIN 566..688
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 378
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 465
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 688 AA; 71859 MW; 6D01EB4F9BBED105 CRC64;
MSSSSSRRRA PHTAQRPATQ RTTAHRRTAA VALAGVAALI AAAVQSGAAS AAPAKPQAGK
MNAAHVAARL TPSQRVELIR HADATRAATA RSLGLGAQEK LVVKDVVKDG DGTLHTRYER
TYAGLPVLGG DLVVDTRSGK TMDVIKATGA TLKVAGLTPA VSKAAAEKQA VQRAKARGGS
KPAADSVRKV IWAASGKPVL AYETVVGGLQ DDGTPNQLHV ITDATTGKKL YEYQGIETGI
GNTQYSGQVN LTTTQSGSSY TLTDGARGGH KTYNLDHGTD GTGTLFSQSN DTWGDGTTSN
AATAGSDAHY GAQETWDFYK DTFGRSGIRN DGVGAYSRVH YGDSYVNAFW DDGCFCMTYG
DGSGNQDPLT SLDVAGHEMS HGVTSNTAGL NYSDESGGLN EATSDIMGTG VEFYANNASD
PGDYLIGEKI NINGDGTPLR YMDKPSKDGN SADSWYSGVG NLDVHYSSGV ANHFFYLLSE
GSGAKTINGV SYDSPTADGL PVTGIGRDKA LQIWYRALTT KFTSTTDYAA ARTGTLAAAG
ELYGTSSNEY NAVQDAWAGV AVGSRSGGGT GGGSTYESNT QVAIPDNGPA VTSDITVSGR
SGKAPSNLQV SVDITHTWRG DLVIDLVGPS GKAYRLKNFS SSDSAHDVKQ TYTVNASAEQ
ANGTWKLRVQ DQATYDTGTI NDWKLTFP
//
