ID V6KE12_STRNV Unreviewed; 459 AA.
AC V6KE12;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Zinc protease {ECO:0000313|EMBL:EST30283.1};
GN ORFNames=M877_09950 {ECO:0000313|EMBL:EST30283.1};
OS Streptomyces niveus NCIMB 11891.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1352941 {ECO:0000313|EMBL:EST30283.1, ECO:0000313|Proteomes:UP000017971};
RN [1] {ECO:0000313|EMBL:EST30283.1, ECO:0000313|Proteomes:UP000017971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 11891 {ECO:0000313|EMBL:EST30283.1,
RC ECO:0000313|Proteomes:UP000017971};
RX PubMed=24407644;
RA Flinspach K., Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT "Draft Genome Sequence of Streptomyces niveus NCIMB 11891, Producer of the
RT Aminocoumarin Antibiotic Novobiocin.";
RL Genome Announc. 2:e01146-e01113(2014).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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:EST30283.1}.
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DR EMBL; AWQW01000072; EST30283.1; -; Genomic_DNA.
DR RefSeq; WP_023538271.1; NZ_CM002280.1.
DR AlphaFoldDB; V6KE12; -.
DR STRING; 193462.BBN63_08200; -.
DR PATRIC; fig|1352941.4.peg.2035; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_3_3_11; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000017971; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851:SF149; GH01077P; 1.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:EST30283.1};
KW Protease {ECO:0000313|EMBL:EST30283.1}.
FT DOMAIN 45..192
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 199..380
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 459 AA; 49541 MW; 738E5A65114B0C50 CRC64;
MTFRSSTTTA RTSSEVRAVA RTQTLLDGQN GIGTVRRTTL PGGLRVVTES LPSVRSATFG
IWVQVGSRDE TPTLNGATHY LEHLLFKGTA KRSALDISSA IDAVGGEMNA FTAKEYTCYY
ARVLDTDLPL AIDVVCDMLT GSLIEAEDVD AERGVILEEI AMTEDDPGDC VHDLFSKTMF
GDTPLGRPVL GTVDTVNALD RARIARFYKK HYDPTHLVVA AAGNVDHDTV VRQVSRAFEK
AGALSRTDAV PVTPREGRRD LRTAGRVDLL DRKTEQAHVV LGMPGLSRTD ERRWALGVLS
TALGGGMSSR LFQEVREKRG LAYSVYSYTS GFADCGLFGV YAGCRPSQVH DVLKICRDGL
DQIASEGLSD EEIGRAVGQL SGSTVLGLED TGALMNRIGK SELCWGTQMS VDDMLARIAA
VTPDDVRAVA RDVLGQRPSL SVIGPLKDKQ ADRLDEAVS
//
