ID C4GJ23_9NEIS Unreviewed; 286 AA.
AC C4GJ23;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Peptidase, M48 family {ECO:0000313|EMBL:EEP67795.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:EEP67795.1};
GN ORFNames=GCWU000324_02045 {ECO:0000313|EMBL:EEP67795.1};
OS Kingella oralis ATCC 51147.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Kingella.
OX NCBI_TaxID=629741 {ECO:0000313|EMBL:EEP67795.1, ECO:0000313|Proteomes:UP000003009};
RN [1] {ECO:0000313|EMBL:EEP67795.1, ECO:0000313|Proteomes:UP000003009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51147 {ECO:0000313|EMBL:EEP67795.1,
RC ECO:0000313|Proteomes:UP000003009};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (APR-2009) 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:EEP67795.1}.
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DR EMBL; ACJW02000003; EEP67795.1; -; Genomic_DNA.
DR AlphaFoldDB; C4GJ23; -.
DR STRING; 629741.GCWU000324_02045; -.
DR HOGENOM; CLU_029002_0_3_4; -.
DR OrthoDB; 15218at2; -.
DR Proteomes; UP000003009; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd07332; 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.
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 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:UP000003009};
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 39..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 87..260
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 286 AA; 32012 MW; 2747F4157DBAC353 CRC64;
MNIFARGLSM QYEAPKFNEK DNPNIPHDTH HGREIRAMLI YLAITVVVIW ALVEVAVRAM
PYVISLPREK QWFSFVGKEL IADKHTQQDP QITALAARLG KHMNLPDNLV TVYISEQEIP
NAYATFGGNV VLYRGLLKEL PSEESVAAVL AHEMAHIKHR DPLRGMSRGL MYSVIAAMLG
SETQIDALVS IGSLKYSRDM ERAADNAAIE AIAKEYGNVG GASQLFATLE EIEQKDHKNH
NIAWLSTHPD TRERQHNVQQ IASQLGYQNS PAKLPNIWQS KSPQTP
//
