ID A4AHA9_9ACTN Unreviewed; 439 AA.
AC A4AHA9;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 80.
DE SubName: Full=Zinc metalloprotease {ECO:0000313|EMBL:EAR25115.1};
GN ORFNames=A20C1_00966 {ECO:0000313|EMBL:EAR25115.1};
OS marine actinobacterium PHSC20C1.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=312284 {ECO:0000313|EMBL:EAR25115.1, ECO:0000313|Proteomes:UP000003868};
RN [1] {ECO:0000313|EMBL:EAR25115.1, ECO:0000313|Proteomes:UP000003868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHSC20C1 {ECO:0000313|EMBL:EAR25115.1,
RC ECO:0000313|Proteomes:UP000003868};
RA Murray A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) 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:EAR25115.1}.
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DR EMBL; AAOB01000004; EAR25115.1; -; Genomic_DNA.
DR AlphaFoldDB; A4AHA9; -.
DR STRING; 312284.A20C1_00966; -.
DR eggNOG; COG0750; Bacteria.
DR HOGENOM; CLU_025778_1_2_11; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000003868; 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; cd00989; PDZ_metalloprotease; 1.
DR CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
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; PF17820; PDZ_6; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 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:EAR25115.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:EAR25115.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003868};
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 133..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 409..430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 146..230
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 439 AA; 46230 MW; 4DB7F9F73DE4ED3A CRC64;
MLLYILGILV VVVGLAVSIG LHEIGHLLPA KLFGVRVSQY MIGFGPTIFS RKRGETEYGV
KAIPLGGYIA MAGMYPPGKA NSKGRTATTG IFQSLVQDAR TASADTLVDV DESRAFYNLP
VLKRVVIMLG GPLMNLLIGI VMFAILFMGF GIAQTTTTIS SVSECVLPAT AERQTCESTD
PEAPGFAAGL LPGDRLVSMD GKPVETWAEA TEYIRAAAGD ELTVVVERAG ADVTLVTEPL
LTERYVYDDR GRIVENAVGE PQTEEYGFLG IGSAVENVKQ PVTAVLPAVG ENVVAVSNVI
LHLPQRMVDV AAAAFGPGDR DPNGPIGVVG VGRIAGEIAS LDSAPVADRI ASLIGLIGSL
NVALFVFNLV PLMPLDGGHV AGALYEGVRR FFAKLFGKPD PGPVDTAKII PLTLVVVVLL
GAMTLLLVYA DIVKPITFF
//
