ID K2IN69_9PROT Unreviewed; 449 AA.
AC K2IN69;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Putative Zn-dependent protease {ECO:0000313|EMBL:EKE71611.1};
GN ORFNames=P24_14659 {ECO:0000313|EMBL:EKE71611.1};
OS Oceanibaculum indicum P24.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Oceanibaculaceae; Oceanibaculum.
OX NCBI_TaxID=1207063 {ECO:0000313|EMBL:EKE71611.1, ECO:0000313|Proteomes:UP000006746};
RN [1] {ECO:0000313|EMBL:EKE71611.1, ECO:0000313|Proteomes:UP000006746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P24 {ECO:0000313|EMBL:EKE71611.1,
RC ECO:0000313|Proteomes:UP000006746};
RX PubMed=23209207; DOI=10.1128/JB.01859-12;
RA Lai Q., Shao Z.;
RT "Genome Sequence of Oceanibaculum indicum Type Strain P24.";
RL J. Bacteriol. 194:6942-6942(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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 -!- 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:EKE71611.1}.
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DR EMBL; AMRL01000022; EKE71611.1; -; Genomic_DNA.
DR RefSeq; WP_008945535.1; NZ_AMRL01000022.1.
DR AlphaFoldDB; K2IN69; -.
DR STRING; 1207063.P24_14659; -.
DR PATRIC; fig|1207063.3.peg.2957; -.
DR eggNOG; COG4783; Bacteria.
DR Proteomes; UP000006746; 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; cd07324; M48C_Oma1-like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR001915; Peptidase_M48.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR PANTHER; PTHR22726:SF1; METALLOENDOPEPTIDASE OMA1, MITOCHONDRIAL; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
DR Pfam; PF13432; TPR_16; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00022792};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:EKE71611.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006746};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 34..226
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT REGION 411..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 449 AA; 49163 MW; 48C54E829537D1B5 CRC64;
MLHKFRVLVA IILSVVIAGL PLPAAAAGMS LIRDTEIENT IRDYATPLFA AAGLQPDNIR
IFIVNSDDIN AFVAGGQNLF LNTGLLVRSD NPNQIMGVIA HETGHIAGGH LARLQDELRR
ASIAQILSMV LGAVAVAASG QGEAGMGVMV GGSEMARRVL LQYNRNQEQA ADQAGVKYLD
AIGQSSRGMV EILEKLSGQE MLLASRQSPY VRSHPLTSER MTFVRNHMAN SPYADAPPPE
GFPMRHKRMV AKLHGFMHPP GRTLMEYPES DTSLPARYAR AIAYYRIPDL NRAVPAIDAL
IAEHPDDPYF HELKGQMLYE NGRVAEAQKA YAEAIERLPD APLIRASHAE TLLALNQEEP
TRRALAELQQ SVRQQPENSR AWRQLAIAHG RLGDTGLAAL ALAEEALLTG QRQTARQQAR
RAQAQLPAGS PGWLRAEDIE TTTRRDAER
//
