ID A0A0B2A561_9MICO Unreviewed; 441 AA.
AC A0A0B2A561;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Zinc metalloprotease {ECO:0000313|EMBL:KHK98649.1};
GN ORFNames=LK09_06800 {ECO:0000313|EMBL:KHK98649.1};
OS Microbacterium mangrovi.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1348253 {ECO:0000313|EMBL:KHK98649.1, ECO:0000313|Proteomes:UP000031030};
RN [1] {ECO:0000313|EMBL:KHK98649.1, ECO:0000313|Proteomes:UP000031030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 115 {ECO:0000313|EMBL:KHK98649.1,
RC ECO:0000313|Proteomes:UP000031030};
RA Lee L.-H.;
RT "Genome sequence of Microbacterium mangrovi MUSC 115(T).";
RL Submitted (NOV-2014) 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:KHK98649.1}.
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DR EMBL; JTDK01000006; KHK98649.1; -; Genomic_DNA.
DR RefSeq; WP_039397366.1; NZ_JTDK01000006.1.
DR AlphaFoldDB; A0A0B2A561; -.
DR STRING; 1348253.LK09_06800; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000031030; 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.
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 ECO:0000313|EMBL:KHK98649.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KHK98649.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031030};
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..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 362..388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 409..430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 182..230
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 441 AA; 46026 MW; DE11F094906C3057 CRC64;
MTVIAFIIGI LLMVVGLAVS IALHELGHLA PAKLFGVRVG QYMIGFGPTL WSRRRGETEY
GIKAIPLGGY ISMAGMYPPS PKGSGDGRAG GGFFATMVQD ARASNDETIA GDEDRVFYKL
PVYQRIIIML GGPVMNLLLA IVLFAIVFSG FGVATATTTV SSVSQCVIPA SENRTTCRAS
DPEAPAAAAG LKPGDTIVSI DGTAVSSFDQ ASAIIQRSPN TQLTFVVERD GQPVTLQVTP
MLAQRAVTNA QGVAEHNADG TVKTENVGFV GIGPTSEMQR QPILAGPQAA LQNVAQVGGL
IWQMPVKVYE TAVTVVTGGE RSADSPMSIV GAGVLAGEVA SADVPVSNRI AGFLSLLASL
NIALFVFNLV PLLPLDGGHV AVALWDGVKR AWARLFRRPP PKPVDATRLV PVTFVVVVAL
IVMGGVLILA DLVNPVSLLG H
//
