CSG1_HALHT
ID CSG1_HALHT Reviewed; 918 AA.
AC G0HV85;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Cell surface glycoprotein 1 {ECO:0000305};
DE AltName: Full=S-layer glycoprotein 1 {ECO:0000303|PubMed:26170448};
DE Flags: Precursor;
GN Name=slg1 {ECO:0000303|PubMed:26170448};
GN OrderedLocusNames=HAH_1991 {ECO:0000312|EMBL:AEM57587.1};
OS Haloarcula hispanica (strain ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182
OS / NCIMB 2187 / VKM B-1755).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=634497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182 / NCIMB 2187 / VKM
RC B-1755;
RX PubMed=21994921; DOI=10.1128/jb.05953-11;
RA Liu H., Wu Z., Li M., Zhang F., Zheng H., Han J., Liu J., Zhou J., Wang S.,
RA Xiang H.;
RT "Complete genome sequence of Haloarcula hispanica, a model haloarchaeon for
RT studying genetics, metabolism, and virus-host interaction.";
RL J. Bacteriol. 193:6086-6087(2011).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION AT ASN-306.
RX PubMed=26170448; DOI=10.1093/glycob/cwv050;
RA Lu H., Lue Y., Ren J., Wang Z., Wang Q., Luo Y., Han J., Xiang H., Du Y.,
RA Jin C.;
RT "Identification of the S-layer glycoproteins and their covalently linked
RT glycans in the halophilic archaeon Haloarcula hispanica.";
RL Glycobiology 25:1150-1162(2015).
CC -!- FUNCTION: S-layer protein. The S-layer is a paracrystalline mono-
CC layered assembly of proteins which coat the surface of the cell. In
CC H.hispanica, the S-layer contains two different glycoproteins, Slg1 and
CC Slg2, which share highly similar amino acid sequences.
CC {ECO:0000269|PubMed:26170448}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall, S-layer
CC {ECO:0000269|PubMed:26170448}. Cell membrane
CC {ECO:0000269|PubMed:26170448}.
CC -!- PTM: N-glycosylated on Asn-306; this N-linked glycan is a branched
CC trisaccharide containing 2-amino-6-sulfo-2,6-dideoxy-glucose
CC (sulfoquinovosamine). {ECO:0000269|PubMed:26170448}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002921; AEM57587.1; -; Genomic_DNA.
DR RefSeq; WP_014040752.1; NC_015948.1.
DR AlphaFoldDB; G0HV85; -.
DR iPTMnet; G0HV85; -.
DR EnsemblBacteria; AEM57587; AEM57587; HAH_1991.
DR GeneID; 11050867; -.
DR KEGG; hhi:HAH_1991; -.
DR eggNOG; arCOG06273; Archaea.
DR HOGENOM; CLU_008482_1_0_2; -.
DR OMA; FAHEANA; -.
DR OrthoDB; 93516at2157; -.
DR Proteomes; UP000005629; Chromosome I.
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; IPR026371; PGF_CTERM.
DR InterPro; IPR026452; Surf_glycop_sig_pep.
DR TIGRFAMs; TIGR04207; halo_sig_pep; 1.
DR TIGRFAMs; TIGR04126; PGF_CTERM; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall; Cell wall biogenesis/degradation; Glycoprotein;
KW Lipoprotein; Membrane; S-layer; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..?
FT /note="Cell surface glycoprotein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000444246"
FT PROPEP ?..918
FT /note="Removed by archaeosortase"
FT /evidence="ECO:0000250|UniProtKB:P25062"
FT /id="PRO_0000444247"
FT TRANSMEM 894..914
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 815..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 895..897
FT /note="PGF sorting signal"
FT /evidence="ECO:0000250|UniProtKB:P25062"
FT COMPBIAS 834..852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..882
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 306
FT /note="N-linked (GalNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:26170448"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 715
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 776
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 836
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 845
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 918 AA; 96693 MW; 75C34C6691407CA6 CRC64;
MTDTNEKIRS LFLTALMVFS VFAGTIAFSG GAAAAANVSV QQAAEYDSGT VELALNGSTG
STVNTGDIDI YVDGNKNPSN YGVSSVDTTD DGTTGRLQFS LDQDVQPNRN LTVKVSGLTG
GDNTVVAEDI DVTSQTIDAD DDSGDTNAFR GEVLAIRADG DTDNDDATSS TKIVVEDSNG
AVVTQDTYTA NSKVYTYETE NLDTGEEYEV SVAGDADENI TISNLDLNVN IDDDVGDGAN
IDDKDTLAVN VSTTRGGEPA NATLFNEDDD KVATQVESLK GNENVVFDFG NQSADDSPYY
VKVTDNQTGV SAESDQINVS ESDDGEASFE SSTVQDNIGD VVNITVQVDN TEDAVINIGD
ENDDNYYIQG QLEDDNGDGE VTVQFNSYTA GNYSDSTVLS VPGDDDIDNI KEGGDYTRGS
LSGDTLEAGS YSMNVTAGTS PDVTSPDTVG TLRLNENSVE NIQTWAAPSD ADIDDDDVDI
YDRIGENLTQ SDDVAAEDVV VHEIQASGIE GALEYEQEDG SASDVTEAFI AATDTTPYRI
NDSDATTSGL RLYVNRTDVG ANADANPIDF SNSSDAVTVV DDPDNNTYFV AVDTSDVVFE
NGKTIVKEED TRLNATFSVR EGPLTDDRNS DSAIYTTSER DATLDLDDSG VVTVSAAAGQ
EVTGETNVAP GSELEVEMES ESDANPFVIR PEVDVATDGT YTATADFQDY SAGTNFTVQT
LDVDGDSDFS DEEDGRIVEA DTATVSISEQ ESDGSEVVVD SAQLSEGGFI AIHAGNASGD
VVGNSEYLGA GSHEDITVTL DEPMDEDFTA VAMPHQDTNG NEAYDFPGDD DPYTQNGSAV
TDSANVTIVE EEQTEAPDTE TETEAPDTET EEETDAPATD EPATDESETT AAEGPGFTAA
IALIALVAAA LLAVRRDN
