ID A0A0P7GXJ1_9EURY Unreviewed; 297 AA.
AC A0A0P7GXJ1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Intramembrane serine protease GlpG {ECO:0000313|EMBL:KPN30214.1};
GN ORFNames=SY89_00940 {ECO:0000313|EMBL:KPN30214.1};
OS Halolamina pelagica.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae.
OX NCBI_TaxID=699431 {ECO:0000313|EMBL:KPN30214.1, ECO:0000313|Proteomes:UP000050535};
RN [1] {ECO:0000313|Proteomes:UP000050535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDK2 {ECO:0000313|Proteomes:UP000050535};
RA Hoang H.T., Killian M.L., Madson D.M., Arruda P.H.E., Sun D.,
RA Schwartz K.J., Yoon K.;
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase S54 family.
CC {ECO:0000256|ARBA:ARBA00009045}.
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:KPN30214.1}.
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DR EMBL; LGUC01000001; KPN30214.1; -; Genomic_DNA.
DR RefSeq; WP_054583274.1; NZ_LGUC01000001.1.
DR AlphaFoldDB; A0A0P7GXJ1; -.
DR STRING; 699431.SY89_00940; -.
DR PATRIC; fig|699431.3.peg.967; -.
DR OrthoDB; 26567at2157; -.
DR Proteomes; UP000050535; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 4.10.1110.10; AN1-like Zinc finger; 1.
DR Gene3D; 1.20.1540.10; Rhomboid-like; 1.
DR InterPro; IPR035896; AN1-like_Znf.
DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR InterPro; IPR000058; Znf_AN1.
DR PANTHER; PTHR43731:SF26; RHOMBOID DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43731; RHOMBOID PROTEASE; 1.
DR Pfam; PF01694; Rhomboid; 1.
DR Pfam; PF01428; zf-AN1; 1.
DR SMART; SM00154; ZnF_AN1; 1.
DR SUPFAM; SSF118310; AN1-like Zinc finger; 1.
DR SUPFAM; SSF144091; Rhomboid-like; 1.
DR PROSITE; PS51039; ZF_AN1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KPN30214.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:KPN30214.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050535};
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};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT TRANSMEM 77..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 216..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..44
FT /note="AN1-type"
FT /evidence="ECO:0000259|PROSITE:PS51039"
FT REGION 278..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 297 AA; 31948 MW; 71F0B538A9968CF1 CRC64;
MATCDECGKQ ENMPYECRRC GGTFCADHRL PENHDCPGLE WDDPVGVFNQ AEERDAGASQ
GSRAGLRRRA RSIWRSYVQN NATFVFLLLM WVTWVTQLLV RNLVSPELEA TLFVLRSTHP
EYVWTWITSV FAHGGIFHIA ANSIGIFFFG QVVERRIGTK RFVALFLASG AVAGLAQIGA
SILLSPAVAT GVVGASGALL AIMGVLTILN PGLTVYLYFF LPVPIWALTI GFAALSLLQG
FGQVGGGAGI AHWAHLAGLA IGLIYGLYVQ DQIEPPRQLQ FGGGGPGGPG RRGGGRF
//