ID A0A0B6WT77_9BACT Unreviewed; 323 AA.
AC A0A0B6WT77;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Zn-dependent protease with chaperone function {ECO:0000313|EMBL:CDM64211.1};
GN ORFNames=PYK22_00203 {ECO:0000313|EMBL:CDM64211.1};
OS Pyrinomonas methylaliphatogenes.
OC Bacteria; Acidobacteriota; Blastocatellia; Blastocatellales;
OC Pyrinomonadaceae; Pyrinomonas.
OX NCBI_TaxID=454194 {ECO:0000313|EMBL:CDM64211.1, ECO:0000313|Proteomes:UP000031518};
RN [1] {ECO:0000313|EMBL:CDM64211.1, ECO:0000313|Proteomes:UP000031518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K22 {ECO:0000313|EMBL:CDM64211.1,
RC ECO:0000313|Proteomes:UP000031518};
RA Stott M.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDM64211.1, ECO:0000313|Proteomes:UP000031518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K22 {ECO:0000313|EMBL:CDM64211.1,
RC ECO:0000313|Proteomes:UP000031518};
RA Lee K.C.Y., Power J.F., Dunfield P.F., Morgan X.C., Huttenhower C.,
RA Stott M.B.;
RT "Complete genome sequence of Pyrinomonas methylaliphatogenes type strain
RT K22T.";
RL Submitted (JAN-2015) 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 -!- SIMILARITY: Belongs to the peptidase M48 family.
CC {ECO:0000256|RuleBase:RU003983}.
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DR EMBL; CBXV010000001; CDM64211.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B6WT77; -.
DR STRING; 454194.PYK22_00203; -.
DR Proteomes; UP000031518; 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; cd07325; M48_Ste24p_like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR001915; Peptidase_M48.
DR PANTHER; PTHR43221; PROTEASE HTPX; 1.
DR PANTHER; PTHR43221:SF3; SLL1280 PROTEIN; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
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:UP000031518};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT DOMAIN 107..304
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 323 AA; 35527 MW; 47D01BC199223EF4 CRC64;
MAIAPDRNGT IRCRYCGQLN QTRAEGTGEA RCGRCRLPLS DRPHKKFPEL NKHEYVHPAD
SRALAALRAI PGIDSALKKF LAVTGESAIR VIFMASAVHV TPKQCPDLYA KLQVACTTLG
VDLPELFVQQ NPTVNAFTGG VERPVIVLHS SLIERLTDEE VLAVIAHEVG HIHAEHVLYL
TAARLLEALA NVALANAPIA KAATTILSGT MRAALLAWAR RAELSCDRAA LLVTQDPDVV
GRTLMKLCGG TFASKVDYRE FLNQARDFQK NYDEHMLDRF WADVISSGLT HPFPVWRVSE
ILRWVDSGEY KRLLNGANAS IDA
//