ID A0A150XI07_9BACT Unreviewed; 433 AA.
AC A0A150XI07;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN ORFNames=AWW68_06085 {ECO:0000313|EMBL:KYG78334.1};
OS Roseivirga spongicola.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Roseivirgaceae;
OC Roseivirga.
OX NCBI_TaxID=333140 {ECO:0000313|EMBL:KYG78334.1, ECO:0000313|Proteomes:UP000075606};
RN [1] {ECO:0000313|EMBL:KYG78334.1, ECO:0000313|Proteomes:UP000075606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UST030701-084 {ECO:0000313|EMBL:KYG78334.1,
RC ECO:0000313|Proteomes:UP000075606};
RA Selvaratnam C., Thevarajoo S., Goh K.M., Ee R., Chan K.-G., Chong C.S.;
RT "Genome sequencing of Roseivirga spongicola UST030701-084.";
RL Submitted (JAN-2016) 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:KYG78334.1}.
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DR EMBL; LRPC01000001; KYG78334.1; -; Genomic_DNA.
DR RefSeq; WP_068217883.1; NZ_LRPC01000001.1.
DR AlphaFoldDB; A0A150XI07; -.
DR STRING; 333140.AWW68_06085; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000075606; 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; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR Gene3D; 2.30.42.10; -; 2.
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; PF02163; Peptidase_M50; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
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:KYG78334.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000075606};
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 101..122
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 359..381
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 410..428
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 10..418
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
SQ SEQUENCE 433 AA; 48032 MW; 4DA15394A45801FF CRC64;
METIVQVAQL LLALSILVGI HEGGHMLTAK MFGMKVEKFF IGFPPTLFSF KKGETEYGLG
AIPLGGFVKI SGMIDESMDK EQMAQPPQPW EFRSKPAWQR LIVMLGGIIV NVIAGVIAFI
ILTYNLGETY LPADLTKQEG IIAGEIAQEA GFETGDKILK VNGEDYDRVS DIWSGETLLA
SNAYWTVERN GEVFDLPVPD GFINKLNDET FELNFIEPRR AIEVEGLQDG FDIPLEKGDR
IVGVNGEEVL FLSDLRVKLE ALVGETATFE ILRNGQSFEY DLPVDERGQI GFVLTNPYQR
DDYTIGEAIP RGTSKAFNAV ILNAKALGRM FGGDVNPRSL SGPIGIVNMF PKTWDWNQFW
YTTGFISMIL AFMNLLPIPA LDGGHVMFLL YEMISGNAPS DKFLEGAQKV GMIFLLVLMV
LVFGNDILKL FNI
//