ID A0A0C1R0J0_9CLOT Unreviewed; 345 AA.
AC A0A0C1R0J0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN Name=rseP {ECO:0000313|EMBL:KIE46907.1};
GN ORFNames=U732_1157 {ECO:0000313|EMBL:KIE46907.1};
OS Clostridium argentinense CDC 2741.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1418104 {ECO:0000313|EMBL:KIE46907.1, ECO:0000313|Proteomes:UP000031366};
RN [1] {ECO:0000313|EMBL:KIE46907.1, ECO:0000313|Proteomes:UP000031366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 2741 {ECO:0000313|EMBL:KIE46907.1,
RC ECO:0000313|Proteomes:UP000031366};
RX PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA Karavis M.A., Smith L.A.;
RT "Genomic sequences of six botulinum neurotoxin-producing strains
RT representing three clostridial species illustrate the mobility and
RT diversity of botulinum neurotoxin genes.";
RL Infect. Genet. Evol. 30:102-113(2014).
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:KIE46907.1}.
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DR EMBL; AYSO01000015; KIE46907.1; -; Genomic_DNA.
DR RefSeq; WP_039631959.1; NZ_AYSO01000015.1.
DR AlphaFoldDB; A0A0C1R0J0; -.
DR STRING; 29341.RSJ17_14405; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000031366; 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; 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; PF13180; PDZ_2; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 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:KIE46907.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031366};
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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 98..119
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 266..284
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 290..307
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 319..336
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 112..184
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 345 AA; 38189 MW; 8B61C4BD76EC9867 CRC64;
MGAMLQNISY VVMGLLAFGL LIVGHEFGHF ILAKLNDVRV DEFSIGMGPK LFGIKGKETE
YMIKALPIGG YVKMYGEDDD VTTSDSRAYA NKSSWQKLSI VSAGPIMNII IAIILFSLVG
KVQGFQIPTV DRIEQNTPAY TAGIRSGDII KEVNGNKIVT WDDFVTNIIT GKGEEVTITI
ERNGIVENYQ VKPEFNKEKN QYLVGIGGAF KKPTFTESIK YGVDQTLSMA KQTFKFFGQL
FQGKISKDDV GGPITIIKVT GKVAKAGLTT LMFFIAYLSV QLAIFNIIPF PALDGGWIML
LLLQIITRKE FNKEKVATIN YYGFMILMAL MVIVLIKDIV SPVQF
//
