CSG_METMA
ID CSG_METMA Reviewed; 669 AA.
AC Q8PVI7;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Major S-layer protein {ECO:0000305};
DE AltName: Full=Cell surface glycoprotein {ECO:0000305};
DE Flags: Precursor;
GN OrderedLocusNames=MM_1976 {ECO:0000312|EMBL:AAM31672.1};
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, SIGNAL PEPTIDE, FUNCTION, SUBCELLULAR
RP LOCATION, AND GLYCOSYLATION.
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=19228054; DOI=10.1021/pr800923e;
RA Francoleon D.R., Boontheung P., Yang Y., Kin U., Ytterberg A.J.,
RA Denny P.A., Denny P.C., Loo J.A., Gunsalus R.P., Loo R.R.;
RT "S-layer, surface-accessible, and concanavalin A binding proteins of
RT Methanosarcina acetivorans and Methanosarcina mazei.";
RL J. Proteome Res. 8:1972-1982(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SIGNAL PEPTIDE.
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=25798134; DOI=10.3389/fmicb.2015.00149;
RA Leon D.R., Ytterberg A.J., Boontheung P., Kim U., Loo J.A., Gunsalus R.P.,
RA Ogorzalek Loo R.R.;
RT "Mining proteomic data to expose protein modifications in Methanosarcina
RT mazei strain Goe1.";
RL Front. Microbiol. 6:149-149(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.
CC {ECO:0000269|PubMed:19228054}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall, S-layer
CC {ECO:0000269|PubMed:19228054}. Cell membrane {ECO:0000305}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:19228054}.
CC -!- SIMILARITY: Belongs to the Methanosarcinales S-layer protein family.
CC {ECO:0000305}.
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DR EMBL; AE008384; AAM31672.1; -; Genomic_DNA.
DR RefSeq; WP_011033908.1; NC_003901.1.
DR AlphaFoldDB; Q8PVI7; -.
DR SMR; Q8PVI7; -.
DR STRING; 192952.MM_1976; -.
DR DNASU; 1480318; -.
DR EnsemblBacteria; AAM31672; AAM31672; MM_1976.
DR GeneID; 24840455; -.
DR KEGG; mma:MM_1976; -.
DR PATRIC; fig|192952.21.peg.2277; -.
DR eggNOG; arCOG03259; Archaea.
DR HOGENOM; CLU_014690_0_0_2; -.
DR OMA; IDYANAM; -.
DR Proteomes; UP000000595; 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; IPR026371; PGF_CTERM.
DR InterPro; IPR006457; S_layer-rel_Mac.
DR Pfam; PF07752; S-layer; 2.
DR TIGRFAMs; TIGR04126; PGF_CTERM; 1.
DR TIGRFAMs; TIGR01567; S_layer_rel_Mac; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall; Cell wall biogenesis/degradation; Glycoprotein;
KW Membrane; Reference proteome; S-layer; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:19228054,
FT ECO:0000269|PubMed:25798134"
FT CHAIN 25..669
FT /note="Major S-layer protein"
FT /id="PRO_0000444300"
FT TRANSMEM 645..665
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 588..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..623
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 600
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 669 AA; 74054 MW; C7F2EC8AAA63A8C4 CRC64;
MKRFAAVSLA ALMLLTVFAS AASAADVIEI RGPVYNGSDI NDIIDTYGEN NALTIDATKF
AAFYYDIDDN VTTETLSILA VPGTEGNVIG EGGIVYETTI QQVDYEFYRP AAGWSNYSLI
GFFAEKYIPI NPDKADKLAK LVLDSDDKYT IRTGEQLDLG EGYSIEAKQV DVDGEKVWLE
FTKDGEFVDD EIISVVSGSD NTWEVELDDI QDEDDVVVLR VHVNQVFQGA VDSIAQIEGL
WLIDYTNAMK IESDDEFGNL DNVKINGDTL TITNEDTFTL TRDDEEEIAE GLFFKTADDT
RALRFYAMKQ ITEPGTYEIR GEVAEGDFSW DATNFAGFFY DVNDDVSTES LTVTGLNGGN
VIPEGGLVYE TTIQMVDYEY SKPSVGWDQF PVLGFFAEEY IPINADKADK LAKLVLDSDD
KYTIRTGEQL DLGEGYAIEA KQVDVDGEKV WLEFTKDGEF VDDEIISVVS GSDNTWEVEL
DDIQDEDDVV VLRVHVNQVF QGAVDSIAQI EGIWLIDYAN AMKIESDDEF GDLDNVKING
ATLTITNEDT FTLTRDDEVE IGQGMFFKVA DTAASDLRYY PFVEKTIDGE VVDDDEDDDN
VTEPVDNDTE VEEPTEEPTE GPTEEPTEGP TTEEPTEEPT EADGTTPGFG VVLGLVGLLA
VVYLVRRNN
