ID A0A428XVY9_9ACTN Unreviewed; 418 AA.
AC A0A428XVY9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Zinc metalloprotease {ECO:0000313|EMBL:RSM59517.1};
GN ORFNames=DMB66_27465 {ECO:0000313|EMBL:RSM59517.1};
OS Actinoplanes sp. ATCC 53533.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1288362 {ECO:0000313|EMBL:RSM59517.1, ECO:0000313|Proteomes:UP000287606};
RN [1] {ECO:0000313|EMBL:RSM59517.1, ECO:0000313|Proteomes:UP000287606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53533 {ECO:0000313|EMBL:RSM59517.1,
RC ECO:0000313|Proteomes:UP000287606};
RA Waglechner N., Wright G.D.;
RT "Evolution of GPA BGCs.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family.
CC {ECO:0000256|ARBA:ARBA00007931}.
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:RSM59517.1}.
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DR EMBL; QHHV01000089; RSM59517.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428XVY9; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000287606; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR42837:SF2; MEMBRANE METALLOPROTEASE ARASP2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR42837; REGULATOR OF SIGMA-E PROTEASE RSEP; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000313|EMBL:RSM59517.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:RSM59517.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000287606};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 99..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 329..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 389..410
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..366
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT DOMAIN 169..225
FT /note="PDZ"
FT /evidence="ECO:0000259|Pfam:PF13180"
SQ SEQUENCE 418 AA; 44964 MW; CFA13F3DC26293B5 CRC64;
MLYWLGTAAF ALAILISVSL HELGHMITAK RYGMKVTQYF VGFGPTIFSF RRGETEYGLK
AIPLGGFCKI VGMTPQDDDV SEADQPRAMW RFPVWKRTVV MSAGSLTHFA LAIVAAWCAA
VFVGLPNPDV PQTVQQQVAL PAQITVADCV QVVLTEQQCK IGTGTDVAAP SAAAGLKTGD
IITKVGEVPI TSYGQLTNVI RATKPGATTF EYTRAGQPGS TTVNLIAAQR PPLDDPKGTV
TEVSVVGISQ SIDIPGTVTY GPVDAIGASL RYDWSLVEGS FVAMKRIPEK IPALWNSITG
SERDPNTPIS VIGASRLGGE AIERGVPEVF LLIFISLNVF IGIFNLLPLL PLDGGHIAIA
WYERVRTWIY GKLHKPDPGR VDYFKLMPLT YAVILIGGAF TLLTATADVI NPITIFSK
//
