ID A0A1R1IKE9_9ACTN Unreviewed; 427 AA.
AC A0A1R1IKE9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:OMG59241.1};
GN ORFNames=BJN44_03545 {ECO:0000313|EMBL:OMG59241.1};
OS Tessaracoccus sp. ZS01.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=1906324 {ECO:0000313|EMBL:OMG59241.1, ECO:0000313|Proteomes:UP000187142};
RN [1] {ECO:0000313|EMBL:OMG59241.1, ECO:0000313|Proteomes:UP000187142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZS01 {ECO:0000313|EMBL:OMG59241.1,
RC ECO:0000313|Proteomes:UP000187142};
RA Salah Z., Rout S.P., Humphreys P.N.;
RT "Range of isolates obtained from hyperalkaline sediments.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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}.
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:OMG59241.1}.
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DR EMBL; MTHC01000001; OMG59241.1; -; Genomic_DNA.
DR RefSeq; WP_076059558.1; NZ_PQFE01000001.1.
DR AlphaFoldDB; A0A1R1IKE9; -.
DR STRING; 1906324.BJN44_03545; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000187142; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
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 SUPFAM; SSF50156; PDZ domain-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000187142};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 122..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 400..421
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..383
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT DOMAIN 177..225
FT /note="PDZ"
FT /evidence="ECO:0000259|Pfam:PF17820"
SQ SEQUENCE 427 AA; 46482 MW; 56054BD924822BB7 CRC64;
MTVLLTVLFA VLFFALIMVS IALHEVGHLV PAKLFGVKVT QYFVGFGKTL WSVRRGETEY
GVKAFPLGGY VRLVGMYPPK RPGAKQTWLT RVADQARSFE WDSIRPEDDG SLFYQKKTWQ
KVIVMLSGPA MNVLLAFLIF LGINVFHGTY QPTLTVGQMW ECVVSAERED RTCTADDPPT
PAVEAGVQVG DTLVSFNGVA LTSWDQMGDL VRTNRDRPAT VVVERDGEEV TLPTVDTVLN
HVPDRLDPTK FVEAGFFGVS PNQELTKAGP LTTAAQMWDM TKQSTVALMS FPARIWSVAA
DLVTGQPRDV NSPISILGAS RVAGEITTTD QLGTADKVAS YLSLLGAVNL FVALLNLVPL
LPLDGGHVAG ALWEWLRRQF ARLRGRPDPG PVDTAKGLPV TYAVGAFLLL GGLVLIAADL
ISPIRLF
//
