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Database: UniProt
Entry: C4KB94_THASP
LinkDB: C4KB94_THASP
Original site: C4KB94_THASP 
ID   C4KB94_THASP            Unreviewed;       271 AA.
AC   C4KB94; A0A5C7SPV4;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=M48 family peptidase {ECO:0000313|EMBL:TXH85844.1};
DE   SubName: Full=Peptidase M48 Ste24p {ECO:0000313|EMBL:ACR01670.1};
GN   OrderedLocusNames=Tmz1t_3072 {ECO:0000313|EMBL:ACR01670.1};
GN   ORFNames=E6Q80_08890 {ECO:0000313|EMBL:TXH85844.1};
OS   Thauera aminoaromatica.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Thauera.
OX   NCBI_TaxID=164330 {ECO:0000313|EMBL:ACR01670.1, ECO:0000313|Proteomes:UP000002186};
RN   [1] {ECO:0000313|Proteomes:UP000002186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MZ1T {ECO:0000313|Proteomes:UP000002186};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sayler G.S.;
RT   "Complete sequence of chromosome of Thauera sp. MZ1T.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACR01670.1, ECO:0000313|Proteomes:UP000002186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MZ1T {ECO:0000313|EMBL:ACR01670.1,
RC   ECO:0000313|Proteomes:UP000002186};
RX   PubMed=23407619; DOI=10.4056/sigs.2696029;
RA   Jiang K., Sanseverino J., Chauhan A., Lucas S., Copeland A., Lapidus A.,
RA   Del Rio T.G., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D.,
RA   Brettin T., Detter J.C., Han C., Chang Y.J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N.C., Mikhailova N., Moser S., Jegier P., Close D.,
RA   Debruyn J.M., Wang Y., Layton A.C., Allen M.S., Sayler G.S.;
RT   "Complete genome sequence of Thauera aminoaromatica strain MZ1T.";
RL   Stand. Genomic Sci. 6:325-335(2012).
RN   [3] {ECO:0000313|EMBL:TXH85844.1, ECO:0000313|Proteomes:UP000321192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bin_27_1 {ECO:0000313|EMBL:TXH85844.1};
RA   Stamps B.W., Spear J.R.;
RT   "Metagenome Assembled Genomes from an Advanced Water Purification
RT   Facility.";
RL   Submitted (SEP-2018) 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}.
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DR   EMBL; CP001281; ACR01670.1; -; Genomic_DNA.
DR   EMBL; SSFD01000128; TXH85844.1; -; Genomic_DNA.
DR   RefSeq; WP_004265813.1; NZ_SSFD01000128.1.
DR   AlphaFoldDB; C4KB94; -.
DR   STRING; 85643.Tmz1t_3072; -.
DR   KEGG; tmz:Tmz1t_3072; -.
DR   eggNOG; COG0501; Bacteria.
DR   HOGENOM; CLU_029002_5_0_4; -.
DR   OrthoDB; 9810445at2; -.
DR   Proteomes; UP000002186; Chromosome.
DR   Proteomes; UP000321192; 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:UP000002186};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..271
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002938159"
FT   DOMAIN          73..257
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   271 AA;  29330 MW;  D1D78A0079DD3AEB CRC64;
     MQSIFKIALP VLLAGTIATA CQTVQTTHGG AVGVQRSQLM MVSAQEVEQA SNQQYQQMVA
     EARSKNALDR DPATVQRVRR IVSRLAAQTG AFRTDAPSWS WEVHVFSSSE LNAWCMAGGK
     MAIYTGLIER LALTDDEIAA VMGHEIAHAL REHARERVSK SMATGLGISV AGALLGVGQL
     GQDLMGQVAK VTFELPNSRE HETEADRMGV ELAARAGYDP RAAVTLWNKM AGQSAGAPPQ
     WLSTHPSHAT RQRDLAEYAA RVIPLYEGAR R
//
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