ID A0A2N4XPD7_9RHOO Unreviewed; 276 AA.
AC A0A2N4XPD7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Peptidase M48 {ECO:0000313|EMBL:PLK48795.1};
GN ORFNames=C0V76_12160 {ECO:0000313|EMBL:PLK48795.1};
OS Uliginosibacterium sp. TH139.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Uliginosibacterium.
OX NCBI_TaxID=2067453 {ECO:0000313|EMBL:PLK48795.1, ECO:0000313|Proteomes:UP000234247};
RN [1] {ECO:0000313|EMBL:PLK48795.1, ECO:0000313|Proteomes:UP000234247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH139 {ECO:0000313|EMBL:PLK48795.1,
RC ECO:0000313|Proteomes:UP000234247};
RA Cai h.;
RT "genomes of bacteria within cyanobacterial aggregates.";
RL Submitted (DEC-2017) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004434}.
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:PLK48795.1}.
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DR EMBL; PKRR01000004; PLK48795.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N4XPD7; -.
DR InParanoid; A0A2N4XPD7; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000234247; 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; cd07331; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW Membrane {ECO:0000256|ARBA:ARBA00022792};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003983};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003983};
KW Reference proteome {ECO:0000313|Proteomes:UP000234247};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT DOMAIN 76..258
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 276 AA; 29973 MW; A0BE81E4CE84B924 CRC64;
MRDKIAPWAS AAVLLAAVVG CQTVQTTNPG VVGVTREQRV SSLIDRGQFN QQSALQYKQV
LGGEQKKGAL NKDPEQVQRI RTIADRLIPQ AEVFRPEAAK WKWEVNVITS KELNAWCMPG
GKIAFYTGLI EGLKASDDEL AQVMGHEIAH ALREHALERA SSAATAGLGM SIIGIALGAS
SGTMDLASVV YNVTFELPNS REHETEADRV GIELAARAGY DPRAAVTLWQ KMGKASEGAP
PKWLSTHPAS ADRQADLKVY GDKVMPLYEQ ARRGNR
//