ID A0A178INN3_9BACT Unreviewed; 479 AA.
AC A0A178INN3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN ORFNames=AW736_03005 {ECO:0000313|EMBL:OAM91442.1};
OS Opitutaceae bacterium TSB47.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX NCBI_TaxID=1184151 {ECO:0000313|EMBL:OAM91442.1, ECO:0000313|Proteomes:UP000078486};
RN [1] {ECO:0000313|EMBL:OAM91442.1, ECO:0000313|Proteomes:UP000078486}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSB47 {ECO:0000313|EMBL:OAM91442.1,
RC ECO:0000313|Proteomes:UP000078486};
RA Wang Y., Shi Y., Qiu Z., Liu S., Yang H.;
RT "High potential of lignocellulose degradation of a new Verrucomicrobia
RT species.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU362031};
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, ECO:0000256|RuleBase:RU362031}.
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:OAM91442.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LRRQ01000027; OAM91442.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178INN3; -.
DR STRING; 1184151.AW736_03005; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000078486; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00989; PDZ_metalloprotease; 2.
DR CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR Gene3D; 2.30.42.10; -; 2.
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 NCBIfam; TIGR00054; RIP metalloprotease RseP; 1.
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; PF17820; PDZ_6; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362031};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362031};
KW Metal-binding {ECO:0000256|RuleBase:RU362031};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU362031}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000078486};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362031};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362031};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU362031}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 107..131
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 387..412
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 432..455
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 234..273
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 479 AA; 51766 MW; DC3ED8D48EA9697B CRC64;
MQFIQAILSN IWAFGLAVFF LGASIFVHEL GHFLAARRRG MKVERFSIGF GPKIFGWRGR
DGIEYRLSWI PLGGYVALPQ LADMAAIEGE SSVAVEKLPP VSYTTKVIVA AAGAFFNVLF
ALVLATIVWV VGQRMLVEEQ TNRVGSVRPI IEATGGKTEP GPAFVAGIKP GDAILAVDGK
KVSSLSDISY LIALGSGRGA QGEPKATLSV QRDGRVFDVD VYPHYVTADE IRDIGIEPSM
QVTVAQVSPG SAAAAAGLLE GDIITHLDGE PVQYESFIRD YIALHKGSAL RITYLRDGKE
SETTAEPRRL VEAAGGEPVY RLGVALRGAY STHIAHIPPW AQFNNIVTLT WRNLSSLVNP
RSDIGLDKMT GPIGIVNQIR VIAKYDFVSV LSFIVLINIS LAIFNLLPIP VLDGGHILFA
TIAKLRGRAL PARFIAATQS VFMLLLLTMI VYVSISDGRR IVRDNRAAAR EAPAAPPEK
//
