ID A0A263CVS3_9PSEU Unreviewed; 408 AA.
AC A0A263CVS3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Zinc metalloprotease {ECO:0000313|EMBL:OZM70223.1};
GN ORFNames=CFN78_26250 {ECO:0000313|EMBL:OZM70223.1};
OS Amycolatopsis antarctica.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1854586 {ECO:0000313|EMBL:OZM70223.1, ECO:0000313|Proteomes:UP000242444};
RN [1] {ECO:0000313|EMBL:OZM70223.1, ECO:0000313|Proteomes:UP000242444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU-G6 {ECO:0000313|EMBL:OZM70223.1,
RC ECO:0000313|Proteomes:UP000242444};
RA Wang J., Leiva S., Huang J., Huang Y.;
RT "Amycolatopsis antarcticus sp. nov., isolated from the surface of an
RT Antarcticus brown macroalga.";
RL Submitted (JUL-2017) 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:OZM70223.1}.
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DR EMBL; NKYE01000022; OZM70223.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A263CVS3; -.
DR InParanoid; A0A263CVS3; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000242444; 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; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR Gene3D; 2.30.42.10; -; 1.
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; 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:OZM70223.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:OZM70223.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000242444};
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 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..368
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
SQ SEQUENCE 408 AA; 43532 MW; A3A1E3D27C4DAFD1 CRC64;
MAAYIFGVVL FALGICISVA LHEAGHMVTA RMFGMRVRRY FVGFGPTVFS FRRKDTEYGL
KAIPLGGFCD IAGFTAMDEV TPEESSRAMW RFKTWKRTVV LAAGSVTHFI VGFIILYAMA
ATMGLPNLAG TPQVAAVAPC VADARTEAEL RTPACGPGTT APALQGGMRA GDEIVSVAGA
ATPSYADVTA KVEPLSGPTP IEVDRDGTIV PLTINVERVD RPVVDPKNPD AAPQVVEKGS
IGVTFPRMFE YNAGTAVGGT LAFTGDMFVQ TFQRLIEFPE RIPAVVEAIF GGERDPNTPV
SVVGASRIGG EAVEQGLWEL FLLLLASLNF FVGVFNLLPL LPLDGGHIAI TWYERVRDMF
RKMRGKAAGG PVDYSKLSAV TMVLVFVGGA VVLLTVTADI VNPIRISP
//
