ID   U5W8U2_9ACTN            Unreviewed;       490 AA.
AC   U5W8U2;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Putative M16-family peptidase {ECO:0000313|EMBL:AGZ45437.1};
GN   ORFNames=AFR_35905 {ECO:0000313|EMBL:AGZ45437.1};
OS   Actinoplanes friuliensis DSM 7358.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ45437.1, ECO:0000313|Proteomes:UP000017746};
RN   [1] {ECO:0000313|EMBL:AGZ45437.1, ECO:0000313|Proteomes:UP000017746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ45437.1,
RC   ECO:0000313|Proteomes:UP000017746};
RX   PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA   Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA   Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT   "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT   HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL   J. Biotechnol. 178:41-42(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}.
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DR   EMBL; CP006272; AGZ45437.1; -; Genomic_DNA.
DR   AlphaFoldDB; U5W8U2; -.
DR   STRING; 1246995.AFR_35905; -.
DR   KEGG; afs:AFR_35905; -.
DR   PATRIC; fig|1246995.3.peg.7267; -.
DR   eggNOG; COG0612; Bacteria.
DR   HOGENOM; CLU_009902_3_3_11; -.
DR   Proteomes; UP000017746; 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:InterPro.
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   Reference proteome {ECO:0000313|Proteomes:UP000017746}.
FT   DOMAIN          79..226
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          235..412
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          35..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          279..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   490 AA;  52244 MW;  79797E5540FFB1CC CRC64;
     MPPPLLRVRT TADARRARTV ARVVRVVASP AAVASVPAAT ATDSRMTESS RGPAERPARV
     STRTLQDGVK KTVLPSGLRI ITEAIPTTRS AALGVWVAVG SRDETPAMSG ASHFLEHLLF
     KGTEKRTALE ISAEIEAVGG ETNAFTTKEY TCYYARVLDA DLPLAVDVLC DAVSRSILDP
     ADVETERGVI LEEIAMHDDE PGDEVHDVFT QAIFGADTPL GRLISGTEET ISPMTRVTIN
     RFYRSRYKAP QVVITAAGNL DHTRVVKLVR AALAGSPFDE GQASPAAKRA SSGGPRPRKP
     TTLVRHRDTE QAHIVLGCAG IDRADERRFA LGVLNNVLGG GMSSRLFQEI REKRGLAYSV
     YSYGSQYADA GLFAVYAGCA PGKAEEVLAL IRAELAVVAA EGITPDELAR GKGMVKGSYV
     LGLEDTGSRM SRLAKSELLH GDLLGVDELL AEVDAVTLDE VNVLAAELLS KPMSLAVVGP
     FDENAFSTPV
//