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Database: UniProt
Entry: A0A1U7EWX1_NATPD
LinkDB: A0A1U7EWX1_NATPD
Original site: A0A1U7EWX1_NATPD 
ID   A0A1U7EWX1_NATPD        Unreviewed;       229 AA.
AC   A0A1U7EWX1;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Probable secreted glycoprotein {ECO:0000313|EMBL:CAI49604.1};
GN   OrderedLocusNames=NP_3026A {ECO:0000313|EMBL:CAI49604.1};
OS   Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS   8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=348780 {ECO:0000313|EMBL:CAI49604.1, ECO:0000313|Proteomes:UP000002698};
RN   [1] {ECO:0000313|EMBL:CAI49604.1, ECO:0000313|Proteomes:UP000002698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 /
RC   NCIMB 2260 / Gabara {ECO:0000313|Proteomes:UP000002698};
RX   PubMed=16169924; DOI=10.1101/gr.3952905;
RA   Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA   Oesterhelt D.;
RT   "Living with two extremes: conclusions from the genome sequence of
RT   Natronomonas pharaonis.";
RL   Genome Res. 15:1336-1343(2005).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004370}. Secreted, cell wall, S-layer
CC       {ECO:0000256|ARBA:ARBA00004237}.
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DR   EMBL; CR936257; CAI49604.1; -; Genomic_DNA.
DR   RefSeq; WP_011323227.1; NC_007426.1.
DR   AlphaFoldDB; A0A1U7EWX1; -.
DR   STRING; 348780.NP_3026A; -.
DR   EnsemblBacteria; CAI49604; CAI49604; NP_3026A.
DR   GeneID; 3701631; -.
DR   KEGG; nph:NP_3026A; -.
DR   eggNOG; arCOG06150; Archaea.
DR   HOGENOM; CLU_1207649_0_0_2; -.
DR   OrthoDB; 157640at2157; -.
DR   Proteomes; UP000002698; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030115; C:S-layer; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR   CDD; cd08547; Type_II_cohesin; 1.
DR   Gene3D; 2.60.40.680; -; 1.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR002102; Cohesin_dom.
DR   InterPro; IPR026371; PGF_CTERM.
DR   NCBIfam; TIGR04126; PGF_CTERM; 1.
DR   Pfam; PF00963; Cohesin; 1.
DR   Pfam; PF18204; PGF-CTERM; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002698};
KW   S-layer {ECO:0000256|ARBA:ARBA00022601};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        204..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          35..150
FT                   /note="Cohesin"
FT                   /evidence="ECO:0000259|Pfam:PF00963"
FT   REGION          170..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..200
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   229 AA;  23747 MW;  12E06CCF1B62262D CRC64;
     MRRLVAVVGC LAVAVAALAG GAAAADSPGL VYFEPDETEA TAGETVDIDA EIRVISVYDN
     EAVESFEYTV EYDPELLSVD DIEEGPWLSG GNETTVAFET DIDEEAGAVT VSQARQPPAG
     GVIGEGTTAT ITFAVAADAP ATNTTVAYTD ASAQMLEYPL PVIETDASIE ISDDGGTTND
     EAEDGPAVTN DADDADDPAP EDQAGFGVVV AIAALFSVVL FGRRRYRML
//
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