ID L9X279_9EURY Unreviewed; 602 AA.
AC L9X279;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Peptidase M50 {ECO:0000313|EMBL:ELY55546.1};
GN ORFNames=C493_11302 {ECO:0000313|EMBL:ELY55546.1};
OS Natronolimnohabitans innermongolicus JCM 12255.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronolimnohabitans.
OX NCBI_TaxID=1227499 {ECO:0000313|EMBL:ELY55546.1, ECO:0000313|Proteomes:UP000011602};
RN [1] {ECO:0000313|EMBL:ELY55546.1, ECO:0000313|Proteomes:UP000011602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 12255 {ECO:0000313|EMBL:ELY55546.1,
RC ECO:0000313|Proteomes:UP000011602};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:ELY55546.1}.
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DR EMBL; AOHZ01000050; ELY55546.1; -; Genomic_DNA.
DR RefSeq; WP_007259541.1; NZ_AOHZ01000050.1.
DR AlphaFoldDB; L9X279; -.
DR STRING; 1227499.C493_11302; -.
DR PATRIC; fig|1227499.3.peg.2309; -.
DR eggNOG; arCOG02834; Archaea.
DR OrthoDB; 15212at2157; -.
DR Proteomes; UP000011602; 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:InterPro.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR001193; MBTPS2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR13325:SF3; MEMBRANE-BOUND TRANSCRIPTION FACTOR SITE-2 PROTEASE; 1.
DR PANTHER; PTHR13325; PROTEASE M50 MEMBRANE-BOUND TRANSCRIPTION FACTOR SITE 2 PROTEASE; 1.
DR Pfam; PF13180; PDZ_2; 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.
DR PROSITE; PS50106; PDZ; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000011602};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 66..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 515..534
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 575..601
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 213..269
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 602 AA; 61315 MW; 0A189A87F8CD3BA3 CRC64;
MLTTLFWIVL GFAVYTALEA RGLLPSWIRV WGPLVTFETT NGLGALDRLA APRHRRRWRV
WTNGGVAVTL ALLVITFGLV LFAAFVALTQ GGASEVNQPR NALAIPGVND FLPLAATPEI
LAGLFVGLFV HEFGHGVLSR VEGISVESAG LIVLAVVPFG AFVGIDEDDE REAETSSRNR
IYAAGIANNL ALAAVAVGCL VLLVSTSIAA VPGVAVGGVY PGTPADEAGL ERGDVITAVD
GERIESDDDH REALEAANDS VELGVEGARD GTKTVTIERS VVVTSALAGS GDGGGDGEAT
ALEPGQTITA VDGEAVATER EFATALENAT VVDLETDDGS GPRTVVAGVA VSDVDSDGAL
AAAGVLDPGD EPDSLVITVL DGERIVDDGD LFDALEDAEP GETVTLEAAV DGEVETYAVT
LGERDGDAAL GVALAPGTSG ITVTDLGVDA HPHEQHLAVL SGDVGAGDGL DASVLAGALA
LFALPFAGMI DGVSSANFGG FVGSVADFYT VTGSLAALEG VVFVVATLLF WAWWLNLLLG
VFNCIPCYPL DGAKILRTTV EDVGSRIGLE SPARVASAAM VGASGLVGVA IALVLASPFL
VG
//
