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Database: UniProt
Entry: A0A1S1Y793_9GAMM
LinkDB: A0A1S1Y793_9GAMM
Original site: A0A1S1Y793_9GAMM 
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}.
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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
//
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