CSG_HALSA
ID CSG_HALSA Reviewed; 852 AA.
AC P0DME1; P08198; Q9HM69;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=Cell surface glycoprotein;
DE AltName: Full=S-layer glycoprotein;
DE Flags: Precursor;
GN Name=csg; OrderedLocusNames=VNG_2679G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [2]
RP REVIEW.
RX PubMed=2673008; DOI=10.1146/annurev.bi.58.070189.001133;
RA Lechner J., Wieland F.;
RT "Structure and biosynthesis of prokaryotic glycoproteins.";
RL Annu. Rev. Biochem. 58:173-194(1989).
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: Glycosylated. {ECO:0000250|UniProtKB:P25062}.
CC -!- PTM: Cleaved by the archaeosortase ArtA at the C-terminus, with removal
CC of a short hydrophobic segment. {ECO:0000250|UniProtKB:P25062}.
CC -!- PTM: Lipidation. {ECO:0000250|UniProtKB:P25062}.
CC -!- SIMILARITY: Belongs to the halobacterial S-layer protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG20702.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE004437; AAG20702.1; ALT_INIT; Genomic_DNA.
DR PIR; A28459; A28459.
DR PIR; B84417; B84417.
DR RefSeq; WP_012289536.1; NC_002607.1.
DR AlphaFoldDB; P0DME1; -.
DR SMR; P0DME1; -.
DR STRING; 64091.VNG_2679G; -.
DR PaxDb; P0DME1; -.
DR EnsemblBacteria; AAG20702; AAG20702; VNG_2679G.
DR GeneID; 5953495; -.
DR KEGG; hal:VNG_2679G; -.
DR PATRIC; fig|64091.14.peg.2081; -.
DR HOGENOM; CLU_015552_0_0_2; -.
DR OrthoDB; 26106at2157; -.
DR Proteomes; UP000000554; 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 3: Inferred from homology;
KW Cell membrane; Cell wall; Cell wall biogenesis/degradation; Glycoprotein;
KW Membrane; Proteoglycan; Reference proteome; S-layer; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000250|UniProtKB:B0R8E4"
FT CHAIN 35..?
FT /note="Cell surface glycoprotein"
FT /id="PRO_0000032616"
FT PROPEP ?..852
FT /note="Removed by archaeosortase"
FT /evidence="ECO:0000250|UniProtKB:P25062"
FT /id="PRO_0000444306"
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 CARBOHYD 36
FT /note="N-linked (GalNAc...) (glycosaminoglycan) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 339
FT /note="N-linked (Glc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 398
FT /note="N-linked (Glc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 438
FT /note="N-linked (Glc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 513
FT /note="N-linked (Glc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 643
FT /note="N-linked (Glc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 727
FT /note="N-linked (Glc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 751
FT /note="N-linked (Glc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 787
FT /note="N-linked (Glc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 789
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 791
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 792
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 793
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 795
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 797
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 798
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 799
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 801
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 802
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 803
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 806
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 807
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 808
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 811
FT /note="N-linked (Glc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 812
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 813
FT /note="O-linked (Gal...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 815
FT /note="N-linked (Glc...) asparagine"
FT /evidence="ECO:0000250"
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
