ID A0A2P8VMY8_9ENTR Unreviewed; 257 AA.
AC A0A2P8VMY8;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Metalloprotease {ECO:0000313|EMBL:PSN08780.1};
GN ORFNames=C7G83_05335 {ECO:0000313|EMBL:PSN08780.1};
OS Siccibacter turicensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Siccibacter.
OX NCBI_TaxID=357233 {ECO:0000313|EMBL:PSN08780.1, ECO:0000313|Proteomes:UP000240212};
RN [1] {ECO:0000313|EMBL:PSN08780.1, ECO:0000313|Proteomes:UP000240212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6100069499-17 {ECO:0000313|EMBL:PSN08780.1,
RC ECO:0000313|Proteomes:UP000240212};
RA Lepuschitz S., Pekard-Amenitsch S., Haunold R., Schill S., Mach R.,
RA Allerberger F., Ruppitsch W., Forsythe S.J.;
RT "Draft genome sequence of the first documented clinical Siccibacter
RT turicensis isolate in Austria.";
RL Submitted (MAR-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:PSN08780.1}.
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DR EMBL; PYEP01000002; PSN08780.1; -; Genomic_DNA.
DR RefSeq; WP_024550798.1; NZ_PYEP01000002.1.
DR AlphaFoldDB; A0A2P8VMY8; -.
DR STRING; 1388748.GCA_000463155_03231; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000240212; 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; cd07334; M48C_loiP_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:SF4; METALLOPROTEASE LOIP; 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 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT DOMAIN 72..245
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT REGION 221..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 257 AA; 27426 MW; CF0A6717F49FA787 CRC64;
MKMRAILLSL GTAALLTGCQ NMDQNGLLSS GAEAYQAYSL SDAQVKTLSD EACKEQDSKA
SLAPANSTYT QRLNKIASAL GDNINGQPVN YKVYVTKDVN AFAMANGCIR VYSGLMDMMN
DNEVEAVIGH EMGHVALGHV KRGMQVALGT NALRVAAASA GGVLGNLSQS QLGALGEKLV
NAQFSQRQEA EADDYSYDLL RKRGINPSGL VTSFEKLAKQ DAGRQSSMFD DHPASEARAQ
HIRDRMKADG LQPPAAQ
//