ID B3QXX9_CHLT3 Unreviewed; 453 AA.
AC B3QXX9;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN OrderedLocusNames=Ctha_1043 {ECO:0000313|EMBL:ACF13507.1};
OS Chloroherpeton thalassium (strain ATCC 35110 / GB-78).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chloroherpetonaceae;
OC Chloroherpeton.
OX NCBI_TaxID=517418 {ECO:0000313|EMBL:ACF13507.1, ECO:0000313|Proteomes:UP000001208};
RN [1] {ECO:0000313|EMBL:ACF13507.1, ECO:0000313|Proteomes:UP000001208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35110 / GB-78 {ECO:0000313|Proteomes:UP000001208};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Chloroherpeton thalassium ATCC 35110.";
RL Submitted (JUN-2008) 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}.
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DR EMBL; CP001100; ACF13507.1; -; Genomic_DNA.
DR RefSeq; WP_012499591.1; NC_011026.1.
DR AlphaFoldDB; B3QXX9; -.
DR STRING; 517418.Ctha_1043; -.
DR KEGG; cts:Ctha_1043; -.
DR eggNOG; COG0750; Bacteria.
DR HOGENOM; CLU_025778_0_0_10; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000001208; Chromosome.
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; 2.
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; 2.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
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:ACF13507.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001208};
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..28
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 104..129
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 382..399
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 433..451
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 123..168
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 453 AA; 49647 MW; 37AA41A707FF2902 CRC64;
MDLFSTIFYF IVAIFILVTV HEFGHFAAAK LFGMRVEKFY IGFDFWNLKL WSTHRGETEY
GIGAIPLGGY VKISGIIDES FDTDFQSRAP EPWEFRSKPV WQRLIVLAAG VIMNMVLAAV
IFIGLALVYG ESKTPITTGA YVEAGSVFED MGIRTGDKIV KVNGKPVKYW DEALDPELFT
HHPLTYTVLR DGKALTFEAP SDIFSRLNGV QVPSMRPIVP PLVAEAFADY PAAKAGLTAG
ALVTKIGGQE IYDWQQVIDN VSANADKPIE IEWKVFGNGK VVEINADKIR KMGVAHTSSI
VPNEQGKIGI TLDQTDLREY AELGFFEAIV AGSKQTWKMT AMTVKGFGRL LSGKEDIRRS
VGGPIKIAKL AGQSAEQGPG SFLLFLAMLS ISLAFLNILP VPALDGGQIV INAVEGIMGR
EVPLNIKLRI QQIGMTALLI LIGFIIFNDI VNP
//
