CSG2_HALHT
ID CSG2_HALHT Reviewed; 922 AA.
AC G0HV86;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Cell surface glycoprotein 2 {ECO:0000305};
DE AltName: Full=S-layer glycoprotein 2 {ECO:0000303|PubMed:26170448};
DE Flags: Precursor;
GN Name=slg2 {ECO:0000303|PubMed:26170448};
GN OrderedLocusNames=HAH_1992 {ECO:0000312|EMBL:AEM57588.1};
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-307.
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-307; 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: O-glycosylated on Thr residues within the DTPE repeats in the C-
CC terminal region; glycans consist of Glc-Gal disaccharides.
CC {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}.
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DR EMBL; CP002921; AEM57588.1; -; Genomic_DNA.
DR RefSeq; WP_014040753.1; NC_015948.1.
DR AlphaFoldDB; G0HV86; -.
DR STRING; 634497.HAH_1992; -.
DR iPTMnet; G0HV86; -.
DR EnsemblBacteria; AEM57588; AEM57588; HAH_1992.
DR GeneID; 23803819; -.
DR KEGG; hhi:HAH_1992; -.
DR eggNOG; arCOG06273; Archaea.
DR HOGENOM; CLU_015552_0_0_2; -.
DR OMA; YARDNND; -.
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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..?
FT /note="Cell surface glycoprotein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000444248"
FT PROPEP ?..922
FT /note="Removed by archaeosortase"
FT /evidence="ECO:0000250|UniProtKB:P25062"
FT /id="PRO_0000444249"
FT TRANSMEM 898..918
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 816..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 899..901
FT /note="PGF sorting signal"
FT /evidence="ECO:0000250|UniProtKB:P25062"
FT COMPBIAS 836..852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..891
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 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 307
FT /note="N-linked (GalNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:26170448"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 587
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 700
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 717
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 809
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 838
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 847
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 922 AA; 96911 MW; 4C5DD2050CEF08CE CRC64;
MTGNSDKVRS LFLTALMVFS VFAGTIAFSG GAAAAANVSV QQAAEYDSGT VELALNGSTG
SPVTTGDINI YIDGNENPSN YGVSSVDTTD DGTTGRLQFS LDQDVQPNRN LTVEVSGLTG
GDNTVVAEDI DVTSQTIDAD DDSGDTNAFR GEVLAIRADG GEGDADDATS STQIVVEDSN
GAVVTQDTYT ANSKVYTYET ENLDTGEEYE VTVGGTADEN ITISNLDLNV NIDDDVGDGA
NIDDTDTLAV NVSTTRGGEP ANATLFNEDD DKVATQIKSL KGNENVVFDF GNQSADDSPY
YVKVTDNQTG VSAESDQINV SESGEGDASF ETSTVQDEVG DVTNITVQMG NTENAVINVG
SQNDDNYVIQ GQLEDDNGDG EVTVQFNSYT AGTDNNNTVL TVPGDDDLDE VEEKGSFTDS
RNSLDEDVLE PQSYSINVTA GTSPDVTSPD TVGTLRLNEN SVESMQTWVA PSDADIDDED
IDIYDRIGEN LTQSDDVAVE DVVVHEIQAS GIEGALEYEQ EDNGSSDVTD AFIAAADTTP
DRINDDTSAS GLQLYVNRTD VGANADADPI NFANSSSAVT VVDDPDNNTY FVALDTEDVE
FESGNTITEE EDTEINATFS VQEGPLTDDS SSESELYTTS ERNAELNLDD DGFVTVGAAA
GQTVSGDTNV APGSELEVEM ESESEANPFV ERPEATVGPN GTYVATEDFS DYSAGTNFTV
QTLDVDGDSD FSDEEDGRIV EADTATVSIS DQESDGSEVV VDSAQLSSGG FIAIHAGDAS
GDVVGNSEYL EAGTYNDLTI TLDEPMDENF TAVAMPHQDT NGNEEYDFPG DDGPYTQNGS
AVTDSANVTV SAEEPEDTPE DTPEDTPEDT PEDTPEDTPA DTPEDTPDTG TETTEAEGPG
FTAAIALIAL VAAALLAVRR DN
