ID A6LCZ7_PARD8 Unreviewed; 265 AA.
AC A6LCZ7;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:ABR43561.1};
GN OrderedLocusNames=BDI_1822 {ECO:0000313|EMBL:ABR43561.1};
OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS 5825 / NCTC 11152).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=435591 {ECO:0000313|EMBL:ABR43561.1, ECO:0000313|Proteomes:UP000000566};
RN [1] {ECO:0000313|EMBL:ABR43561.1, ECO:0000313|Proteomes:UP000000566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152
RC {ECO:0000313|Proteomes:UP000000566};
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(2007).
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 -!- SIMILARITY: Belongs to the peptidase M48 family.
CC {ECO:0000256|RuleBase:RU003983}.
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; CP000140; ABR43561.1; -; Genomic_DNA.
DR RefSeq; WP_005854995.1; NC_009615.1.
DR AlphaFoldDB; A6LCZ7; -.
DR STRING; 435591.BDI_1822; -.
DR PaxDb; 435591-BDI_1822; -.
DR DNASU; 5306972; -.
DR KEGG; pdi:BDI_1822; -.
DR PATRIC; fig|435591.13.peg.1809; -.
DR eggNOG; COG0501; Bacteria.
DR HOGENOM; CLU_074068_0_1_10; -.
DR BioCyc; PDIS435591:G1G5A-1874-MONOMER; -.
DR Proteomes; UP000000566; Chromosome.
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; cd07334; M48C_loiP_like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR001915; Peptidase_M48.
DR PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR PANTHER; PTHR22726:SF8; METALLOPROTEASE YCAL; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003983};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003983};
KW Reference proteome {ECO:0000313|Proteomes:UP000000566};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..265
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002698722"
FT DOMAIN 90..255
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT REGION 235..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 265 AA; 28844 MW; 46DAA255F64EAE5B CRC64;
MKKILLSLAF LAGVSLTVSA QFKIGGKTIN TKKVINAATD VAHAATLSDE DVAKMAKEYI
QWMDTHNEVA GPDTEMGQRL ERLTANVKKV SGLDLNFKVY NVVDVNAFAC GDGSVRVCGG
LMKIMDDDEV FAVIGHEIGH VVHSDSKDAM KNAYLTSAAK NAAGAVSGTV SKLTDSQLGD
MAQALAGAQY SQKQEYEADE FGFQFCIDYG RDPYGMSNSL NKLLQLSESE AKSSKFMQMF
SSHPETQKRA DRVKEKADEY VKSKQ
//
