ID A0A1X3CHJ4_9NEIS Unreviewed; 276 AA.
AC A0A1X3CHJ4;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Peptidase, M48 family {ECO:0000313|EMBL:VEJ21968.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:VEJ21968.1};
GN Name=yggG {ECO:0000313|EMBL:VEJ21968.1};
GN ORFNames=NCTC12227_01735 {ECO:0000313|EMBL:VEJ21968.1};
OS Neisseria animaloris.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=326522 {ECO:0000313|EMBL:VEJ21968.1, ECO:0000313|Proteomes:UP000268229};
RN [1] {ECO:0000313|EMBL:VEJ21968.1, ECO:0000313|Proteomes:UP000268229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12227 {ECO:0000313|EMBL:VEJ21968.1,
RC ECO:0000313|Proteomes:UP000268229};
RG Pathogen Informatics;
RL Submitted (DEC-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; LR134516; VEJ21968.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X3CHJ4; -.
DR STRING; 326522.BWD08_08885; -.
DR KEGG; nani:NCTC12227_01735; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000268229; Chromosome 1.
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:UP000268229};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..276
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030037421"
FT DOMAIN 64..254
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 276 AA; 30106 MW; BE2710B8CDEBA8FD CRC64;
MKSPTFRLSA LMVSAVLALS GCTSVADIVG YDSATLNESA AKSYTQVMQQ AKSKRILDTT
SHTSRRIQTV FNRLKPYAEQ ANQTGVPFRW EMSVIKSDEL NAWAMPGGKM AMYTGMVDRL
KLSDDEIAAV VGHEMTHALL EHSKKAIGQQ VLTGLAADIG GSLISGKAGV SSDIVGLSSN
ILSQYGVNMP FSRSQEREAD AGGVRLMAQA GYNPQAAITV WEKMNRISDN NNTWNAITSS
HPTNNARIQA IRNMLPEVMP IYERNKRGQN IPKRNS
//
