ID A0A2U3AE20_9BACL Unreviewed; 416 AA.
AC A0A2U3AE20;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN Name=rasP {ECO:0000313|EMBL:STX09116.1};
GN ORFNames=NCTC10597_00786 {ECO:0000313|EMBL:STX09116.1};
OS Kurthia zopfii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Kurthia.
OX NCBI_TaxID=1650 {ECO:0000313|EMBL:STX09116.1, ECO:0000313|Proteomes:UP000254330};
RN [1] {ECO:0000313|EMBL:STX09116.1, ECO:0000313|Proteomes:UP000254330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10597 {ECO:0000313|EMBL:STX09116.1,
RC ECO:0000313|Proteomes:UP000254330};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU362031};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family.
CC {ECO:0000256|ARBA:ARBA00007931, ECO:0000256|RuleBase:RU362031}.
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:STX09116.1}.
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DR EMBL; UGNP01000001; STX09116.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U3AE20; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000254330; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; cd00989; PDZ_metalloprotease; 1.
DR CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR NCBIfam; TIGR00054; RIP metalloprotease RseP; 1.
DR PANTHER; PTHR42837:SF2; MEMBRANE METALLOPROTEASE ARASP2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR42837; REGULATOR OF SIGMA-E PROTEASE RSEP; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362031};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362031};
KW Metal-binding {ECO:0000256|RuleBase:RU362031};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU362031};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:STX09116.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362031};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362031};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU362031}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 171..192
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 338..360
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 389..408
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
SQ SEQUENCE 416 AA; 46654 MW; 582A7042244EA2AE CRC64;
MQAAIAFILV FGSIVFFHEL GHFIFAKRSG ILVREFAIGF GPKIIGITRG ETLYTVRLLP
MGGYVRMAGE DMDTVELQPG YRIGFLLNDQ DEITRIVLNQ NKQLPDMLFL EVEKADLLKG
LWVEGYDEEE QLVRYNVARD AVIEENGKDT IIAPYERTFD AKSLPKRAMT IFAGPLFNFI
LAVVFFIIIA LVQGMPTNEP LIANVVPGSP AQQAGIQKDD VIIGANGEKI EKYEELSEII
KDNKNKEIKL NVQRGDEKVT LGVTPKLNKD KVVQIGIQYA NKYEKNPLKA ISYGFEQTYN
WFIKIAELLG LLVTGHFTLD ALSGPVGIYK ATEEVAQYGF MTLMNWAAVL SINLGIMNLL
PLPALDGGRL LFFAYEAVRG RPIDKQKEGV VHFVGFALLM ILMIAVTWND IQKFFF
//
