ID A0A1S1Y793_9GAMM Unreviewed; 330 AA.
AC A0A1S1Y793;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Peptidase M48 domain-containing protein {ECO:0000259|Pfam:PF01435};
GN ORFNames=BJL95_21715 {ECO:0000313|EMBL:OHX37364.1};
OS Methylomonas sp. LWB.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=1905845 {ECO:0000313|EMBL:OHX37364.1, ECO:0000313|Proteomes:UP000180009};
RN [1] {ECO:0000313|EMBL:OHX37364.1, ECO:0000313|Proteomes:UP000180009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LWB {ECO:0000313|EMBL:OHX37364.1,
RC ECO:0000313|Proteomes:UP000180009};
RA Stephenson J., Kumaresan D., Hillebrand-Voiculescu A.M., Murrell J.C.;
RT "Draft genome sequence of the methane oxidising bacterium Candidatus
RT Methylomonas sp. LWB isolated from Movile Cave.";
RL Submitted (OCT-2016) 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}.
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:OHX37364.1}.
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; MKMC01000012; OHX37364.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S1Y793; -.
DR Proteomes; UP000180009; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd07332; M48C_Oma1_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:SF1; METALLOENDOPEPTIDASE OMA1, MITOCHONDRIAL; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW Membrane {ECO:0000256|SAM:Phobius};
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:UP000180009};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT TRANSMEM 86..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 169..328
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 330 AA; 36183 MW; BC82D7B396CD5411 CRC64;
MYFDGRQAIA HRVVLSVEAG HLQLRGETVN RSEPLTALTI PAPLGRSPRL ILFSDGARCE
VADSVGFADL LPERADGWLS TLESHIVAAI TAVLLLLGLA IAGYRWGLPY AAETVAERLP
AEMLTEMDHQ LFASLDQHWL QPSGVPESRR ADIQAKAFSL APHAEVRLAF RASRQLGANA
FALPGGTVLV LDDLVGLTAN DDEIVAVLAH EFGHVREKHA LRQMLQATVV GLALAAYLGD
ISSLLAAAPA VLLETGYSRD FERSADRYAA DLLISHHQSP TLLADMLDKL DAYWRERDRL
QLGDRKGEFG EYWSTHPDNA ERIAFLRGQR
//