CSG_HALS3
ID CSG_HALS3 Reviewed; 852 AA.
AC B0R8E4; P08198; Q9HM69;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Cell surface glycoprotein;
DE AltName: Full=S-layer glycoprotein;
DE Flags: Precursor;
GN Name=csg; OrderedLocusNames=OE_4759F;
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 35-55; 509-519;
RP 626-645 AND 787-796, LACK OF GLYCOSYLATION AT ASN-51, AND GLYCOSYLATION AT
RP ASN-36; ASN-513 AND ASN-643.
RC STRAIN=R1M1;
RX PubMed=3036870; DOI=10.1016/s0021-9258(18)47994-x;
RA Lechner J., Sumper M.;
RT "The primary structure of a procaryotic glycoprotein. Cloning and
RT sequencing of the cell surface glycoprotein gene of halobacteria.";
RL J. Biol. Chem. 262:9724-9729(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
RN [3]
RP IDENTIFICATION.
RX PubMed=1270419; DOI=10.1016/s0021-9258(17)33647-5;
RA Mescher M.F., Strominger J.L.;
RT "Purification and characterization of a prokaryotic glycoprotein from the
RT cell envelope of Halobacterium salinarium.";
RL J. Biol. Chem. 251:2005-2014(1976).
RN [4]
RP PROTEIN SEQUENCE OF 770-778, AND LIPIDATION.
RC STRAIN=R1M1;
RX PubMed=10364251; DOI=10.1074/jbc.274.25.18011;
RA Kikuchi A., Sagami H., Ogura K.;
RT "Evidence for covalent attachment of diphytanylglyceryl phosphate to the
RT cell-surface glycoprotein of Halobacterium halobium.";
RL J. Biol. Chem. 274:18011-18016(1999).
CC -!- FUNCTION: S-layer protein. The S-layer is a paracrystalline mono-
CC layered assembly of proteins which coat the surface of the cell.
CC {ECO:0000250|UniProtKB:P25062}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall, S-layer
CC {ECO:0000250|UniProtKB:P25062}. Cell membrane
CC {ECO:0000250|UniProtKB:P25062}.
CC -!- PTM: N-linked glycan at Asn-36 consists of a glycosaminoglycan chain,
CC constructed by a repeating sulfated pentasaccharide block composed of
CC GlcNAc, GalNAc, Gal, GalA, 3-O-methyl-GalA, and sulfate in the molar
CC ratio of 1:1:1:1:1:2; the other N-linked glycans contain Glc, GlcA and
CC IdoA. {ECO:0000269|PubMed:3036870}.
CC -!- PTM: O-linked glycans consist of Glc-Gal disaccharides.
CC {ECO:0000269|PubMed:3036870}.
CC -!- PTM: The C-terminus (residues 770-778) is lipidated with
CC diphytanylglyceryl phosphate. {ECO:0000269|PubMed:10364251}.
CC -!- PTM: Cleaved by the archaeosortase ArtA at the C-terminus, with removal
CC of a short hydrophobic segment. {ECO:0000250|UniProtKB:P25062}.
CC -!- SIMILARITY: Belongs to the halobacterial S-layer protein family.
CC {ECO:0000305}.
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DR EMBL; J02767; AAA72185.1; -; Genomic_DNA.
DR EMBL; AM774415; CAP15013.1; -; Genomic_DNA.
DR RefSeq; WP_012289536.1; NC_010364.1.
DR AlphaFoldDB; B0R8E4; -.
DR SMR; B0R8E4; -.
DR iPTMnet; B0R8E4; -.
DR EnsemblBacteria; CAP15013; CAP15013; OE_4759F.
DR GeneID; 5953495; -.
DR KEGG; hsl:OE_4759F; -.
DR HOGENOM; CLU_015552_0_0_2; -.
DR OMA; YARDNND; -.
DR Proteomes; UP000001321; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; 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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR InterPro; IPR026458; Major_cell_surface_glycoprot.
DR InterPro; IPR026371; PGF_CTERM.
DR InterPro; IPR026452; Surf_glycop_sig_pep.
DR TIGRFAMs; TIGR04207; halo_sig_pep; 1.
DR TIGRFAMs; TIGR04216; halo_surf_glyco; 1.
DR TIGRFAMs; TIGR04126; PGF_CTERM; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Glycoprotein; Lipoprotein; Membrane;
KW Proteoglycan; S-layer; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000269|PubMed:3036870"
FT CHAIN 35..?
FT /note="Cell surface glycoprotein"
FT /id="PRO_0000428763"
FT PROPEP ?..852
FT /note="Removed by archaeosortase"
FT /evidence="ECO:0000250|UniProtKB:P25062"
FT /id="PRO_0000444305"
FT TRANSMEM 829..849
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 84..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 830..832
FT /note="PGF sorting signal"
FT /evidence="ECO:0000250|UniProtKB:P25062"
FT COMPBIAS 780..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 51
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:3036870"
FT CARBOHYD 36
FT /note="N-linked (GalNAc...) (glycosaminoglycan) asparagine"
FT /evidence="ECO:0000269|PubMed:3036870"
FT CARBOHYD 339
FT /note="N-linked (Glc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 398
FT /note="N-linked (Glc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 438
FT /note="N-linked (Glc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 513
FT /note="N-linked (Glc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3036870"
FT CARBOHYD 643
FT /note="N-linked (Glc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3036870"
FT CARBOHYD 727
FT /note="N-linked (Glc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 751
FT /note="N-linked (Glc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 787
FT /note="N-linked (Glc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 789
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 791
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 792
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 793
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 795
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 797
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 798
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 799
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 801
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 802
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 803
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 806
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 807
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 808
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 811
FT /note="N-linked (Glc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 812
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 813
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 815
FT /note="N-linked (Glc...) asparagine"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="S -> F (in Ref. 1; AAA72185)"
FT /evidence="ECO:0000305"
FT CONFLICT 648
FT /note="S -> P (in Ref. 1; AAA72185)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="L -> V (in Ref. 1; AAA72185)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 852 AA; 89758 MW; BBEE867569B226CD CRC64;
MTDTTGKLRA VLLTALMVGS VIGAGVAFTG GAAAANASDL NDYQRFNENT NYTYSTASED
GKTEGSVASG ATIFQGEEDV TFRKLDNEKE VSPATLSRTG GSDEGVPLQM PIPEDQSTGS
YDSNGPDNDE ADFGVTVQSP SVTMLEVRNN ADNDVTGGVL NTQQDESSIA VDYNYYAAED
LELTVEDEDG LDVTDEILAA DQSGGAYEDG TGNNGPNTLR FDIDPNNVDA GDYTVSVEGV
EDLDFGDATE SASVTISSSN KASLNLAEDE VVQGANLKYT IENSPEGNYH AVTIDSSDFR
DSSSGADAAK VMRSVGDTVD TGLVVDNDST TEIVDDYENT SISDVDYAYA IVEIDDGNGV
GSIETQYLDD SSADIDLYPA SDTEDAPDYV NSNEELTNGS ALDGVSTDDD TDFDVTQGDI
TLDNPTGAYV VGSEVDINGT ANEGTDDVVL YARDNNDFEL VTVDGEKSIE VDSDDTFEEE
DITLSDGDKG GDDILGLPGT YRLGIIAKSD AVNSSGGVKD NIDTSDFNQG VSSTSSIRVT
DTELTASFET YNGQVADDDN QIDVEGTAPG KDNVAAIIIG SRGKVKFQSI SVDSDDTFDE
EDIDISELRQ GSASAHILSS GRDGKFGEDT ANSISDLEDE VGNYTSGSPT GDQIRDRILS
NTVDDTASDD LIVTQQFRLV DGLTTIEATE GGEAGGSLTV MGTTNRKADD NTITVELLQG
DASIEINSTD EWNSDGQWSV DVPLSNVEPG NYTVEADDGD NTDRQNVEIV EELEEPDQTT
VDQPENNQTM TTTMTETTTE TTTEMTTTQE NTTENGSEGT SDGESGGSIP GFGVGVALVA
VLGAALLALR QN
