ID A0A175Y1Z4_9SPHN Unreviewed; 457 AA.
AC A0A175Y1Z4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Peptidase M48 {ECO:0000313|EMBL:KZB94376.1};
GN ORFNames=AVM11_07900 {ECO:0000313|EMBL:KZB94376.1};
OS Sphingomonas melonis TY.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=621456 {ECO:0000313|EMBL:KZB94376.1, ECO:0000313|Proteomes:UP000078460};
RN [1] {ECO:0000313|EMBL:KZB94376.1, ECO:0000313|Proteomes:UP000078460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TY {ECO:0000313|EMBL:KZB94376.1,
RC ECO:0000313|Proteomes:UP000078460};
RA Wang H., Zhu P.;
RT "Sphingomonas melonis TY, whole genome shotgun sequencing.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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:KZB94376.1}.
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DR EMBL; LQCK02000034; KZB94376.1; -; Genomic_DNA.
DR RefSeq; WP_017977551.1; NZ_LQCK02000034.1.
DR AlphaFoldDB; A0A175Y1Z4; -.
DR SMR; A0A175Y1Z4; -.
DR STRING; 621456.BJP26_05570; -.
DR GeneID; 67489651; -.
DR OrthoDB; 9814887at2; -.
DR Proteomes; UP000078460; 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 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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 45..226
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 457 AA; 48994 MW; 479AF35CD02ECD9B CRC64;
MIARVPALKR LVIAAAASVL LAAQPAYAQS ILRDAETEAM FADMSTPLVK AAGLSPRDVK
VVLINDDSIN AFVAGGQTVY VHSGLLQAAT SANQVQGVIA HELGHIADGH VVLADAGIKP
AMHITLLSMV LGLAAVAAGA GEAGAGLMAL GQQAGMGKYL SFSRTQESSA DAAGARFLTT
AGITGKGMLT FFKTLQQQEY RYGVENIDPF MQTHPLSGER IANLTAVLTA APSWNTPPNP
ALEERFRRVK AKLEGYVMPP ERTLRDFPDT DTSIYAHYAR AYAYHKAGYP DKADAESLAL
IKAKPDDPYF QEIRGQILLE AGKPADAIAP LRAATEGSRN NPLIATTFGH ALIATEDKTH
YPEAIRVLRV ATGRDDQNPF AWYQLGTAYE LTGDTARAAL ATAERASMDG DMRTAAQSAR
YALANIPKNT PDWIRAQDIA MAAQNDMDDN PKKYKKR
//
