ID A0A368NFS7_9GAMM Unreviewed; 269 AA.
AC A0A368NFS7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=M48 family peptidase {ECO:0000313|EMBL:RCU48773.1};
GN ORFNames=DU002_13355 {ECO:0000313|EMBL:RCU48773.1};
OS Corallincola holothuriorum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Psychromonadaceae; Corallincola.
OX NCBI_TaxID=2282215 {ECO:0000313|EMBL:RCU48773.1, ECO:0000313|Proteomes:UP000252558};
RN [1] {ECO:0000313|EMBL:RCU48773.1, ECO:0000313|Proteomes:UP000252558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C4 {ECO:0000313|EMBL:RCU48773.1,
RC ECO:0000313|Proteomes:UP000252558};
RA Xia H.;
RT "Corallincola holothuriorum sp. nov., a new facultative anaerobe isolated
RT from sea cucumber Apostichopus japonicus.";
RL Submitted (JUL-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}.
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:RCU48773.1}.
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DR EMBL; QPID01000008; RCU48773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368NFS7; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000252558; 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:UP000252558};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..269
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016867462"
FT DOMAIN 62..246
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 269 AA; 28609 MW; FBC6530BD820D90A CRC64;
MSISITKSAV SLCAIAVLAA CTASPTGRDQ ILLYSDQEMS SLGGQSFEQI KQQEKISGDS
SLNRYVQCVA RHITAQVPQQ YHQAGWEVVV FDSEQANAFA LPGGKIGVYT GLLKIAQNQD
QLAAVIGHEV GHVMADHSNE RLTHNQLAGV TMAVAGAAIA ASDSDDSAMW MAALGLGVQV
GVMLPYSRTQ ESESDVIGLD LMAQAGFDPT QSVALWRNMA KASSGQPPEF FSTHPSHDTR
IADLESNMSR AQGIAAKAHN KGLNPKCRL
//
