ID D2ZY96_NEIMU Unreviewed; 255 AA.
AC D2ZY96;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Peptidase, M48 family {ECO:0000313|EMBL:EFC87868.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:EFC87868.1};
GN ORFNames=NEIMUCOT_05603 {ECO:0000313|EMBL:EFC87868.1};
OS Neisseria mucosa ATCC 25996.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=546266 {ECO:0000313|EMBL:EFC87868.1, ECO:0000313|Proteomes:UP000003344};
RN [1] {ECO:0000313|EMBL:EFC87868.1, ECO:0000313|Proteomes:UP000003344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25996 {ECO:0000313|EMBL:EFC87868.1,
RC ECO:0000313|Proteomes:UP000003344};
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 (OCT-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:EFC87868.1}.
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DR EMBL; ACDX02000013; EFC87868.1; -; Genomic_DNA.
DR RefSeq; WP_003743511.1; NZ_ACDX02000013.1.
DR AlphaFoldDB; D2ZY96; -.
DR STRING; 546266.NEIMUCOT_05603; -.
DR GeneID; 61323893; -.
DR eggNOG; COG0501; Bacteria.
DR Proteomes; UP000003344; 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:UP000003344};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..255
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003041221"
FT DOMAIN 62..242
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 255 AA; 27533 MW; E12B8CCE29FD4E6C CRC64;
MNKISKKYGL WLGVAALAGC TSVADMVGYD TAALNEGAER NYTQVVQKAR SQNALDVSSP
TAQRVHRVFS RLVPYANRAN RTGIPFNWQM NVIRSNDLNA WAMPGGKMAV YTGMVERLQL
TDDEIAAVIG HEMTHALLEH SKKAIGGQVL TGLGGSILAG AVGLDGNLVG VGTDLLATKP
FSRHQESEAD AGGVRLMAQA GYNPQAAISV WEKMNRVQGG SQVAILSTHP ANNTRIEAIR
RMLPEVMPIY HQNKR
//
