ID A0A1W9RGG8_9BACT Unreviewed; 340 AA.
AC A0A1W9RGG8;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=PDZ domain-containing protein {ECO:0000259|SMART:SM00228};
GN ORFNames=B6D53_01905 {ECO:0000313|EMBL:OQX83669.1};
OS Candidatus Omnitrophica bacterium 4484_49.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1970784 {ECO:0000313|EMBL:OQX83669.1, ECO:0000313|Proteomes:UP000192833};
RN [1] {ECO:0000313|Proteomes:UP000192833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dombrowski N., Seitz K., Teske A., Baker B.;
RT "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT hydrothermal sediment communities.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003983};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003983};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004434}.
CC -!- SIMILARITY: Belongs to the peptidase M48 family.
CC {ECO:0000256|RuleBase:RU003983}.
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:OQX83669.1}.
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DR EMBL; NATI01000019; OQX83669.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9RGG8; -.
DR Proteomes; UP000192833; Unassembled WGS sequence.
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; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001915; Peptidase_M48.
DR PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR PANTHER; PTHR22726:SF1; METALLOENDOPEPTIDASE OMA1, MITOCHONDRIAL; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW Membrane {ECO:0000256|ARBA:ARBA00022792};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003983};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003983};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT DOMAIN 87..154
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 340 AA; 37604 MW; E73960893A1008AA CRC64;
MKSVFLNLLI LGLILSGCVT TTGPYVSPGE VYQTAEELKV KALKFRLQKE KKVAEVGYRL
LKSIKEKLGS YPYIGARFIK VDDYVRRLFG ITSTYPYAIA YCVNGSPAYK AGLQPGDVIK
EINGIRIYSP SALGSVLRNI KPGERVNFIV IRGDKEVYLN FVTGEIPADV TFRMVDEESV
NAGATSNQVV VTYGLMRFIN SDDELAIILG HELAHIIRGH IAKRMGTDLL AVLLGIAAGY
GAESISPGSG DVVMQGVGSA FSSYYSREFE READYYGILY AYRAGYDIHA GIDVWERFAV
EVPQSLTRDF FSTHPTSAER LLRIKKIVQE LEAEGKIPSR
//
