ID A0A1L8ZD94_BORBI Unreviewed; 432 AA.
AC A0A1L8ZD94;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, 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=ER70_01020 {ECO:0000313|EMBL:OJH15696.1};
OS Borrelia bissettiae (Borreliella bissettiae).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borreliella.
OX NCBI_TaxID=64897 {ECO:0000313|EMBL:OJH15696.1, ECO:0000313|Proteomes:UP000183624};
RN [1] {ECO:0000313|EMBL:OJH15696.1, ECO:0000313|Proteomes:UP000183624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO275 {ECO:0000313|EMBL:OJH15696.1,
RC ECO:0000313|Proteomes:UP000183624};
RX PubMed=26419825; DOI=10.1099/mic.0.000192;
RA Leydet B.F.Jr., Liang F.T.;
RT "Similarities in murine infection and immune response to Borrelia bissettii
RT and Borrelia burgdorferi sensu stricto.";
RL Microbiology 161:2352-2360(2015).
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:OJH15696.1}.
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DR EMBL; JNBW01000051; OJH15696.1; -; Genomic_DNA.
DR RefSeq; WP_071890867.1; NZ_JNBW01000051.1.
DR AlphaFoldDB; A0A1L8ZD94; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000183624; 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; -; 2.
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; 2.
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:OJH15696.1};
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 98..127
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 338..356
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 362..389
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 401..422
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 115..185
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT DOMAIN 192..265
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 432 AA; 49096 MW; 33DC7D8261CCF120 CRC64;
MYILFSVLAL SFIIFIHELG HFLFAKLFKV KVEVFSVGIG PSILKFKINN TEYRLSPILL
GGYCKLKGFD HLEKELKANK ELKADKDSLF GISHFKKILI YFAGPLFNLI FSFVVFIFIS
MAGVIYFDYS SRVSVLNKDS FLKDKFRDGD VILKVNNKKI EYFSDLRKVI PEEKSTVTFN
VLREKENITF KETVGLQDFL KEIGPWVDLV ISDVVLNSPA KIAGMKSGDE IISIDNILLK
NKRDLDDLLK NLDSDAVEIK FSRNGEIFSS KLVFHDKNKM IGIYFSPPLK RIVKVENVSS
AIKNSFFKVV NALQDILYSI FLLITNFLNT SKSVSGPVGI LGILSSSYSL GLLYWINSIS
FLSLILAGMN LFFIVIPIFD GGQIFISFVE LLRGKRFKAK TIYSFYSFGI FLGLFLFGLG
LFNDLKDLFN IF
//
