CSG_HALJT
ID CSG_HALJT Reviewed; 862 AA.
AC Q9C4B4; M0LCE2;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-AUG-2020, sequence version 2.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Cell surface glycoprotein {ECO:0000303|Ref.3};
DE AltName: Full=S-layer glycoprotein;
DE Flags: Precursor;
GN Name=csg {ECO:0000303|Ref.3};
GN ORFNames=C444_08390 {ECO:0000312|EMBL:EMA31256.1};
OS Haloarcula japonica (strain ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032
OS / NCIMB 13157 / TR-1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=1227453;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1;
RX PubMed=9680334; DOI=10.1007/s007920050012;
RA Wakai H., Nakamura S., Kawasaki H., Takada K., Mizutani S., Aono R.,
RA Horikoshi K.;
RT "Cloning and sequencing of the gene encoding the cell surface glycoprotein
RT of Haloarcula japonica strain TR-1.";
RL Extremophiles 1:29-35(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 35-52, FUNCTION, SUBCELLULAR LOCATION, AND
RP GLYCOSYLATION.
RC STRAIN=ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1;
RA Nakamura S., Mizutani S., Wakai H., Kawasaki H., Aono R., Horikoshi K.;
RT "Purification and partial characterization of cell surface glycoprotein
RT from extremely halophilic archaeon Haloarcula japonica strain TR-1.";
RL Biotechnol. Lett. 17:705-706(1995).
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:0000305|PubMed:9680334, ECO:0000305|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall, S-layer
CC {ECO:0000305|PubMed:9680334, ECO:0000305|Ref.3}. Cell membrane
CC {ECO:0000250|UniProtKB:P25062}.
CC -!- PTM: Glycosylated. {ECO:0000269|Ref.3}.
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=EMA31256.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D87290; BAB39352.1; -; Genomic_DNA.
DR EMBL; AOLY01000022; EMA31256.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_049909326.1; NZ_AOLY01000022.1.
DR AlphaFoldDB; Q9C4B4; -.
DR SMR; Q9C4B4; -.
DR EnsemblBacteria; EMA31256; EMA31256; C444_08390.
DR PATRIC; fig|1227453.3.peg.1659; -.
DR eggNOG; arCOG03906; Archaea.
DR Proteomes; UP000011524; Unassembled WGS sequence.
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; NAS:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; NAS:UniProtKB.
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; S-layer;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 35..?
FT /note="Cell surface glycoprotein"
FT /id="PRO_0000032615"
FT PROPEP ?..862
FT /note="Removed by archaeosortase"
FT /evidence="ECO:0000250|UniProtKB:P25062"
FT /id="PRO_0000444189"
FT TRANSMEM 838..858
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 35..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 839..841
FT /note="PGF sorting signal"
FT /evidence="ECO:0000250|UniProtKB:P25062"
FT COMPBIAS 41..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..831
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 702
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 761
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 369
FT /note="V -> A (in Ref. 1; BAB39352)"
FT CONFLICT 691
FT /note="T -> I (in Ref. 1; BAB39352)"
SQ SEQUENCE 862 AA; 90636 MW; DA0F2CDC7D82858E CRC64;
MTDTQQKIKA VLLTVLMVTS VFAATIAFSG AAAASERGAG DSYTTGPTDG NQDNVDSAGN
VGAGAVVFQG EDDIEGEFAD GNGDTVGIGE LQKVSGDNEG ILLESPIPQD QPTGRYTANP
GVEGTEGVTL QTPRITDLEI QNSDEGDVTG SILQANNDNT AEILVDYNYD EAEDLELTVE
DEDGLEVTEE ILADGASETV NTNVNNDDHP NPAADGDRDD SFDAGFTINP SNVDEGEYTI
TVEGVEDLDF GDASETATVE ITTDQTASLS LDSDEVTQGE DLGFDIENSP EGNFHAVVIE
ESEFRDSASA SNYAKVFRNV GDTSDRGLVG EDADGNTVAV APGDADSLES IDYAYGIVEI
DGGTGVGSVE TQYLDDSSID IDLYEAANGD YTDNNAHVND INLVTDDTYE TDDEQDFDVL
EGDLTIDSPS GTYVTGSEVD VNGTASEGID DVAIYARDNN DYELVEIDSE ETISVDGDDT
FSEEDISLSG GDLGGNDILG LPGTYRIGVV DVEDADSNSN GTVDDSLTTS EFNSGVSSAE
SLRVTDTELN GTFITYNGQI SSDDNQIDVE GQAPGKDNLV IAFVDSRGNA VATDISVDDD
DTFSEDDISI SALSEGTVTA HIISSGRDNL FGDGVSDSSS GFASLIEEEY ASGSSTGDQV
RSRILENSVD DTASDDLIVN EQFRLADGLT TVESVNSPVE ANGTIEIEGT TNRKPDDNTI
TVELLDDEDE SVTVDSTDEW SSDGQWSVSL DLSDENVEPG NFTVEADDGD NTDRQSVQIV
EAGSLEEEQP ATDTPEPDTD TPEPATDTPE PATDTPEPDT DTPEPDTETE EATTEATGPG
FTAAIALIAL VAAALLAVRR DN
