ID A0A148N6B1_9GAMM Unreviewed; 441 AA.
AC A0A148N6B1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Peptidase S41 {ECO:0000313|EMBL:KXJ40084.1};
GN ORFNames=AXA67_13690 {ECO:0000313|EMBL:KXJ40084.1};
OS Methylothermaceae bacteria B42.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylothermaceae.
OX NCBI_TaxID=1798802 {ECO:0000313|EMBL:KXJ40084.1, ECO:0000313|Proteomes:UP000074680};
RN [1] {ECO:0000313|EMBL:KXJ40084.1, ECO:0000313|Proteomes:UP000074680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B42 {ECO:0000313|EMBL:KXJ40084.1};
RX PubMed=26779119; DOI=10.3389/fmicb.2015.01425;
RA Skennerton C.T., Ward L.M., Michel A., Metcalfe K., Valiente C., Mullin S.,
RA Chan K.Y., Gradinaru V., Orphan V.J.;
RT "Genomic Reconstruction of an Uncultured Hydrothermal Vent
RT Gammaproteobacterial Methanotroph (Family Methylothermaceae) Indicates
RT Multiple Adaptations to Oxygen Limitation.";
RL Front. Microbiol. 6:1425-1425(2015).
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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:KXJ40084.1}.
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DR EMBL; LSNW01000032; KXJ40084.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A148N6B1; -.
DR STRING; 1798802.AXA67_13690; -.
DR Proteomes; UP000074680; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00988; PDZ_CTP_protease; 1.
DR CDD; cd07560; Peptidase_S41_CPP; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.750.44; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
DR InterPro; IPR005151; Tail-specific_protease.
DR NCBIfam; TIGR00225; prc; 1.
DR PANTHER; PTHR32060:SF22; CARBOXYL-TERMINAL-PROCESSING PEPTIDASE 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004404};
KW Protease {ECO:0000256|RuleBase:RU004404};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}.
FT DOMAIN 90..158
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 383..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 441 AA; 48248 MW; E0BB4B5130FE552F CRC64;
MRKTTNLFLI ALGAFLGILL GTCGSVLAER EAKKAETIPF VELKTFTEVF GRIQQDYVEP
VTDKKLLENA IRGMLTGLDP HSSYLSPDQY KELRIGTTGQ FGGLGIEVTM ENGFVKVIAP
IDDTPAQKAG IKPGDLIIRL DEKPVKGMSL QDAVKIMRGK PGTDIVLTIV REGEDKPLKI
KITRDIIKIK SVKSKLLEKG YGYLRITSFQ SRTGSQMLKE IKKLRKKGDL KGIVLDLRNN
PGGVLNAAVA VSDAFLDQGL IVYTDGRIED AKMKFEATPG DILRDVPMVV LINTGSASAS
EIVAGALQDH KRAIIMGQKS FGKGSVQTIL PLSNGGAIKL TTARYYTPSG RSIQAEGIVP
DIPLGTIRLE TIAEAEEFKP LTEADLSRHL ENGTKPEKEK KESGKQEKND KENEMLLKDY
PLHEALNVLK GINIAKQSLK K
//
