ID V6KEL0_STRNV Unreviewed; 451 AA.
AC V6KEL0;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:EST30527.1};
GN ORFNames=M877_09415 {ECO:0000313|EMBL:EST30527.1};
OS Streptomyces niveus NCIMB 11891.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1352941 {ECO:0000313|EMBL:EST30527.1, ECO:0000313|Proteomes:UP000017971};
RN [1] {ECO:0000313|EMBL:EST30527.1, ECO:0000313|Proteomes:UP000017971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 11891 {ECO:0000313|EMBL:EST30527.1,
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 -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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:EST30527.1}.
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DR EMBL; AWQW01000065; EST30527.1; -; Genomic_DNA.
DR AlphaFoldDB; V6KEL0; -.
DR STRING; 193462.BBN63_07680; -.
DR PATRIC; fig|1352941.4.peg.1927; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_1_1_11; -.
DR Proteomes; UP000017971; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
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; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 26..159
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 184..364
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 430..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 49227 MW; 2EE0BF0749724800 CRC64;
MGHTATAQAG SGGLTATEHR LANGLRVVLS EDHLTPVAAV CLWYDVGSRH EVKGRTGLAH
LFEHLMFQGS KQVKGNGHFE LVQGAGGSLN GTTSFERTNY FETMPTHQLE LALWLEADRM
GSLLSSLDDE GMENQRDVVK NERRQRYDNV PYGTAFERLT ALSYPEGHPY HHTPIGSMAD
LDAATLDDAR QFFRTYYAPN NAVLSVVGDI DPEQTLAWVE KYFGSIPGHD GKQPPRDGSL
PDTIGGQLRE EIHEDVPARA LMAAYRLPQD GTREADAADL ALTVLGGGES SRLHNRLVRH
DRTAVAAGFG LLRLAGAPSL GWLDVKTSGG VEVPQIEAAV DEELARFAAD GPTAEEMERA
QAQLEREWLD RLGTVAGRAD ELCRYAVLFG DPQLALTAVQ RVLDVTADEV REVAAARLRP
DNRAVLVYEP TTADDEDVAD EITDEHEGAD K
//
