ID A0A2U1CB95_9BURK Unreviewed; 396 AA.
AC A0A2U1CB95;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Zn-dependent protease with chaperone function {ECO:0000313|EMBL:PVY58183.1};
GN ORFNames=C8D04_3497 {ECO:0000313|EMBL:PVY58183.1};
OS Simplicispira sp. 125.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Simplicispira.
OX NCBI_TaxID=2135643 {ECO:0000313|EMBL:PVY58183.1, ECO:0000313|Proteomes:UP000245599};
RN [1] {ECO:0000313|EMBL:PVY58183.1, ECO:0000313|Proteomes:UP000245599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=125 {ECO:0000313|EMBL:PVY58183.1,
RC ECO:0000313|Proteomes:UP000245599};
RA Chistoserdova L.;
RT "Synthetic bacterial communities of pure cultures isolated from sediment of
RT Lake Washington, USA.";
RL Submitted (APR-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 -!- 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:PVY58183.1}.
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DR EMBL; QEKM01000001; PVY58183.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1CB95; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000245599; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
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:UP000245599};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT TRANSMEM 119..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 219..386
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 396 AA; 42481 MW; 6640376CF6449455 CRC64;
MNTSPESTSA PGDLLPGRWF DGRSSKARPV VVGLQPTPQG PSLVLHPLSP PGAAPVVFTS
TQVDWPEAWN ERRPPLRVVV DLRDHGSVEI DAVAQWRAAL AAAGNRPGIA QRMQTRWPAL
LGVALAAVVG LALFYRYGTP WAATQLTRFV PLSWETSVAQ SALQQMDDGT LKPSTLPRAR
QDALKARLDA LVRQTPASLH RYHGYRPPLS LEFRAGMGAN AFALPGGKIV MTDGIVKAAA
DKGLPDDALV GVLAHEIGHV VHRHTTRMVV EQGVLQMGLG LALGDVSTMV STGSALLTGL
HYRRSHEREA DCYAIGLMRH AALPTAPMGQ LLLAMAHEEE AQAKKSDAPA SAADKGKARA
DAKAHPVWSL LSSHPDTIQR ATELQQGQAP YCPQMY
//
