CSG_HALGI
ID CSG_HALGI Reviewed; 855 AA.
AC A0A0K1IRS6;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 1.
DT 25-MAY-2022, entry version 15.
DE RecName: Full=Cell surface glycoprotein {ECO:0000305};
DE AltName: Full=S-layer glycoprotein {ECO:0000303|PubMed:29558455};
DE Flags: Precursor;
GN ORFNames=ABY42_04395 {ECO:0000312|EMBL:AKU07018.1};
OS Haloferax gibbonsii.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=35746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARA6;
RX PubMed=26299206; DOI=10.1016/j.jbiotec.2015.08.010;
RA Pinto L.H., D'Alincourt Carvalho-Assef A.P., Vieira R.P., Clementino M.M.,
RA Albano R.M.;
RT "Complete genome sequence of Haloferax gibbonsii strain ARA6, a potential
RT producer of polyhydroxyalkanoates and halocins isolated from Araruama, Rio
RT de Janeiro, Brasil.";
RL J. Biotechnol. 212:69-70(2015).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29558455; DOI=10.3390/genes9030172;
RA Shalev Y., Soucy S.M., Papke R.T., Gogarten J.P., Eichler J., Gophna U.;
RT "Comparative analysis of surface layer glycoproteins and genes involved in
RT protein glycosylation in the genus Haloferax.";
RL Genes (Basel) 9:172-172(2018).
CC -!- FUNCTION: S-layer protein. The S-layer is a paracrystalline mono-
CC layered assembly of proteins which coats the surface of the cell.
CC {ECO:0000305|PubMed:29558455}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall, S-layer
CC {ECO:0000269|PubMed:29558455}. Cell membrane {ECO:0000305}.
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}.
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DR EMBL; CP011947; AKU07018.1; -; Genomic_DNA.
DR RefSeq; WP_050458809.1; NZ_CP011947.1.
DR AlphaFoldDB; A0A0K1IRS6; -.
DR EnsemblBacteria; AKU07018; AKU07018; ABY42_04395.
DR GeneID; 25245174; -.
DR KEGG; hgi:ABY42_04395; -.
DR PATRIC; fig|35746.4.peg.933; -.
DR Proteomes; UP000066124; 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 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; Glycoprotein; Membrane; S-layer; Secreted;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..?
FT /note="Cell surface glycoprotein"
FT /id="PRO_0000444353"
FT PROPEP ?..855
FT /note="Removed by archaeosortase"
FT /evidence="ECO:0000250|UniProtKB:P25062"
FT /id="PRO_0000444354"
FT TRANSMEM 831..851
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 782..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 832..834
FT /note="PGF sorting signal"
FT /evidence="ECO:0000250|UniProtKB:P25062"
FT COMPBIAS 783..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..824
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 588
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 608
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 642
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 656
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 754
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 855 AA; 89168 MW; 0872B7C641F04E00 CRC64;
MTANKQVRAV LLAALMVFSV FAGSIAFTGT AAAAATSATV SPDTVDKGPS ASVDVTVNSG
GANDVHVWLD LNDDGYYNAS EPNSTDTAAA TATLSLSIPE SVSAGEYNVS AAESASLTAG
TTQQEAYDTL DVVAANPADF NSATHFDDGT PKVEVAFDEA VTVNEMNVTD GETNLSQSVS
VSSGQVNVTL SQVYTDDLEV TYNVTDTSGN TATATEDVTF APIYVANESN NTAYQGSNVA
VVASAVDTDV EVEGADDDNN YQFSGSTGPN SQVFVFDTDG KTLDTYQFTV GGAQKAQVDV
RDLGLELTVD DLNITTKDGI EGSVSANAGD RTVDIVALDD DGDEVEDTET TVTLNGQGEA
DFNLSSVDAG EYTIEATDAF TGVTLESDTV TVSKAKDSTG DFASSVINEQ VGDVAEITVT
LDGTDTGTVT IGDYSLGYSA NVTVEDDNDD GEVVLLFNSY APKKTSSFDV DDSDDEYTVE
DITTDIPSGE TLDAGDYDLE VATGGEADNV ATLVLEDRST DSVATWTAPT GADLTETEDV
YDAIENENLT QTDSLANGDV VVTQVSATGL EGAFDASNFD ALSGTQFNLT VEQTNPGPNR
DAKVLGINSS SATIIADGDN DTYFIVYDLD DVSASRTDYY DNTSTLYEVE DDDAFNATFT
VLEDGDLAED DESASDEFEV VTPELELDQD EFAVGNAAEQ SISGTATVAP GTELTIRVTS
DGDTQPRFLK TASVYVQADG TFSSAFDFSE QNLNDTFEVT ASVDSGTADD ATADGIVGEA
METTTAAETT TTEESTETTT TEESTEEPTE TATATEEPTE EATEETTESS TPGFGVVVAL
VALVAAALLA VRRDN
