ID A0A3S5B5Y6_9NEIS Unreviewed; 334 AA.
AC A0A3S5B5Y6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 28-JAN-2026, entry version 28.
DE SubName: Full=Uncharacterized metalloprotease yggG {ECO:0000313|EMBL:VEJ51889.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:VEJ51889.1};
GN Name=yggG_2 {ECO:0000313|EMBL:VEJ51889.1};
GN ORFNames=NCTC12742_01798 {ECO:0000313|EMBL:VEJ51889.1};
OS Neisseria weaveri.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Neisseriaceae; Neisseria.
OX NCBI_TaxID=28091 {ECO:0000313|EMBL:VEJ51889.1, ECO:0000313|Proteomes:UP000272771};
RN [1] {ECO:0000313|EMBL:VEJ51889.1, ECO:0000313|Proteomes:UP000272771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12742 {ECO:0000313|EMBL:VEJ51889.1,
RC ECO:0000313|Proteomes:UP000272771};
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 -!- SIMILARITY: Belongs to the peptidase M48 family.
CC {ECO:0000256|RuleBase:RU003983}.
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DR EMBL; LR134533; VEJ51889.1; -; Genomic_DNA.
DR RefSeq; WP_004283627.1; NZ_CAUJRG010000005.1.
DR AlphaFoldDB; A0A3S5B5Y6; -.
DR STRING; 28091.SAMEA3174300_00355; -.
DR KEGG; nwe:SAMEA3174300_0355; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000272771; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:TreeGrafter.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:TreeGrafter.
DR CDD; cd07332; M48C_Oma1_like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR055518; DUF7092.
DR InterPro; IPR051156; Mito/Outer_Membr_Metalloprot.
DR InterPro; IPR001915; Peptidase_M48.
DR PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR PANTHER; PTHR22726:SF1; METALLOENDOPEPTIDASE OMA1, MITOCHONDRIAL; 1.
DR Pfam; PF23368; DUF7092; 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:UP000272771};
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 98..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..78
FT /note="DUF7092"
FT /evidence="ECO:0000259|Pfam:PF23368"
FT DOMAIN 188..331
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 334 AA; 37026 MW; 88D2ADD8AA351D15 CRC64;
MSESLTVSYY DGKRNVPHQA EISLDGGKLR VVYNGGQTAE YPLHSIAYMA GVGGVLPALE
LPGDARIEFL NHDVPHWLPL QNKIMLKQVG RLEKSWKWAA VSLVAMICVV AVVFKWGIPA
AAYHAAHHLP EKTLQGVGNQ AEEIILELTG ETKLSAKRRR EISDLYYQKL KPENPAKLLF
REGGELGANA FAIPNNTIML TDALVDLAKH DHEILAVLAH EQGHLKERHS LQQALRGIGM
SVFLLTLTGD ATDIIDGLPV LFATAKYSQE FELEADLHAI NELKRLNIPP QHLADFLQRL
HQAHGHGDEN SAEHILSTHP VTSERVKQVE QHAK
//
