ID   A0A1A7QDW4_9SPHN        Unreviewed;       364 AA.
AC   A0A1A7QDW4;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Peptidase M48 domain-containing protein {ECO:0000259|Pfam:PF01435};
GN   ORFNames=A9995_13095 {ECO:0000313|EMBL:OBX18175.1};
OS   Erythrobacter sp. QSSC1-22B.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=1860125 {ECO:0000313|EMBL:OBX18175.1, ECO:0000313|Proteomes:UP000092728};
RN   [1] {ECO:0000313|EMBL:OBX18175.1, ECO:0000313|Proteomes:UP000092728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QSSC1-22B {ECO:0000313|EMBL:OBX18175.1,
RC   ECO:0000313|Proteomes:UP000092728};
RA   Bowman J.P.;
RT   "Draft genome of Erythrobacter sp. QSSC1-22B.";
RL   Submitted (JUN-2016) 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   -!- 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:OBX18175.1}.
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DR   EMBL; LZRP01000008; OBX18175.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A7QDW4; -.
DR   STRING; 1860125.A9995_13095; -.
DR   Proteomes; UP000092728; 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; cd07332; M48C_Oma1_like; 1.
DR   Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR   InterPro; IPR001915; Peptidase_M48.
DR   PANTHER; PTHR22726:SF25; BETA-BARREL ASSEMBLY-ENHANCING PROTEASE; 1.
DR   PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR   Pfam; PF01435; Peptidase_M48; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003983};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003983};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092728};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT   DOMAIN          155..328
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
FT   REGION          289..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   364 AA;  39130 MW;  AD516CF3AAC82BF7 CRC64;
     MIPVVWYDGV TALRREGTAS WSGDRLLLVE TGGAQHTVPF TDLRFVESLR QEQVYGRESL
     PDFRLRLPLD LPPEFERHLP APSRYGGWID RLGLGKAVVV FGVASAAAVA LFMTAPEWLG
     PRVPESFEAR IGEAMIGNFG NRLCSTPEGD AALAKLLDAV DPADRQVRAG IANIDMVNAV
     ALPGGQVMLF DGLVQQAESP AELAGVLGHE VGHVRERHVM TALLRQFGLS ILLSGANSGL
     GDTVFGLAAM GYTRDAEREA DEFARARMAQ SNVSPLGAAE FFERMAKESG AGTDDDADDD
     ADNGSGTDIT GWIASHPSAG SRARAYRNAA TEGANYDPIL TPSEFEDLKG MCEADPDVEE
     FEFF
//