ID A0A2W1ZJU5_9MICO Unreviewed; 439 AA.
AC A0A2W1ZJU5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:PZF60000.1};
GN ORFNames=DEJ23_02165 {ECO:0000313|EMBL:PZF60000.1};
OS Curtobacterium sp. MCSS17_008.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=2175647 {ECO:0000313|EMBL:PZF60000.1, ECO:0000313|Proteomes:UP000248620};
RN [1] {ECO:0000313|EMBL:PZF60000.1, ECO:0000313|Proteomes:UP000248620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCSS17_008 {ECO:0000313|EMBL:PZF60000.1,
RC ECO:0000313|Proteomes:UP000248620};
RA Chase A.B., Gomez-Lunar Z., Lopez A.E., Li J., Allison S.D., Martiny A.C.,
RA Martiny J.B.H.;
RT "Emergence of Soil Bacterial Ecotypes Along a Climate Gradient.";
RL Submitted (JUN-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:PZF60000.1}.
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DR EMBL; QKSM01000001; PZF60000.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W1ZJU5; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000248620; 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:InterPro.
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.
DR PROSITE; PS50106; PDZ; 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 Protease {ECO:0000256|ARBA:ARBA00022670};
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 127..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 411..429
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 180..228
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 439 AA; 46021 MW; BFD3945C4E979025 CRC64;
MLLFVLGVVV FIIGLLVSIG LHELGHLSFA KLFNVKVTQY SLGFGKAIWS FRRGETEYGI
RPILLGGYIS MVGMLKPRAT GRPNAITNTG MYGAFVQDAR QASAEQIADA GGDDSRAFYR
LTPWKRIIVM VAGPAMNLVI GIVLFGVLLC GFGAPTTTFT SSVDCVLPTS QSTRCAPGDG
SSPAKEAGIR DGDVVLAVNG TQDPTIAEVS RVFKRSAGKA VTVVVERDGQ RRTLEVTPQL
ATRDVVTDRG TVAKNADGST KTQQVGVVGV SIGQSLVRQS PAAVLPATGA QIAASAHLII
DLPQRLVAVW NAAFGAEERS QDSPVSVVGV GRAIGEVSSM SGVPVVDKAY TILGLLASLN
IGLFVLNMVP LLPLDGGHIA GALWEAVKRR AHQLAGKPDP GAIDLAKSMP LTMVVVVLLA
GMSALLIYAD LVRPVDLFG
//