ID A0A0M5JJ30_9GAMM Unreviewed; 258 AA.
AC A0A0M5JJ30;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=M48 family metallopeptidase {ECO:0000313|EMBL:QPF38886.1};
DE SubName: Full=Type I deoxyribonuclease HsdR {ECO:0000313|EMBL:ALD01302.1};
GN ORFNames=AMQ28_02375 {ECO:0000313|EMBL:ALD01302.1}, H0S58_05165
GN {ECO:0000313|EMBL:QPF38886.1};
OS Acinetobacter sp. TTH0-4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1646498 {ECO:0000313|EMBL:ALD01302.1, ECO:0000313|Proteomes:UP000055186};
RN [1] {ECO:0000313|EMBL:ALD01302.1, ECO:0000313|Proteomes:UP000055186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTH0-4 {ECO:0000313|EMBL:ALD01302.1,
RC ECO:0000313|Proteomes:UP000055186};
RA Zhang G.;
RT "Acinetobacter qinghaiensis sp. nov., isolated from active layer of
RT permafrost region.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QPF38886.1, ECO:0000313|Proteomes:UP000594614}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1BD1 {ECO:0000313|EMBL:QPF38886.1,
RC ECO:0000313|Proteomes:UP000594614};
RA Ghaly T.M., Sajjad A., Tetu S.G., Gillings M.R.;
RT "A family of multi-drug resistance mega-plasmids in Acinetobacter
RT species.";
RL Submitted (JUL-2020) 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; CP012608; ALD01302.1; -; Genomic_DNA.
DR EMBL; CP059079; QPF38886.1; -; Genomic_DNA.
DR RefSeq; WP_053578187.1; NZ_CP059079.1.
DR AlphaFoldDB; A0A0M5JJ30; -.
DR KEGG; att:AMQ28_02375; -.
DR PATRIC; fig|1646498.3.peg.487; -.
DR Proteomes; UP000055186; Chromosome.
DR Proteomes; UP000594614; Chromosome.
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 Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..258
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033720014"
FT DOMAIN 63..246
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 258 AA; 27124 MW; 0B49F64605C19460 CRC64;
MNNKLILSLC VAGIVTISGC TTVADMAGAD SATLNVAAAQ GFNKTIQEAS ANKTLDTSSA
TYRRINSVFS RLKPYGDQIN QTGQKFNWQL AVLKSDQVNA YVAPGGKVVF YTGIVNKLNL
TDAEIAAVMG HEMVHALEEH SKNKIGAQAL TNLALNIGLS AAGNNVGQLG AAAAQLGSQV
GVGLPYSRSL ESQADQGGLL LMARAGYNPQ AAITLWEKMN KLDGAGGSSF LSTHPSNSQR
IEAMRKNLPA AQAIYNKR
//
