CSG_METBF
ID CSG_METBF Reviewed; 668 AA.
AC Q46BP2;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Major S-layer protein {ECO:0000303|PubMed:22666082};
DE AltName: Full=Cell surface glycoprotein {ECO:0000305};
DE Flags: Precursor;
GN Name=slmA1 {ECO:0000303|PubMed:22666082};
GN OrderedLocusNames=Mbar_A1758 {ECO:0000312|EMBL:AAZ70700.1};
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, AND
RP GLYCOSYLATION.
RC STRAIN=Fusaro / DSM 804;
RX PubMed=22666082; DOI=10.1155/2012/873589;
RA Rohlin L., Leon D.R., Kim U., Loo J.A., Ogorzalek Loo R.R., Gunsalus R.P.;
RT "Identification of the major expressed S-layer and cell surface-layer-
RT related proteins in the model methanogenic archaea: Methanosarcina barkeri
RT Fusaro and Methanosarcina acetivorans C2A.";
RL Archaea 2012:873589-873589(2012).
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:22666082}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall, S-layer
CC {ECO:0000269|PubMed:22666082}. Cell membrane {ECO:0000305}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:22666082}.
CC -!- SIMILARITY: Belongs to the Methanosarcinales S-layer protein family.
CC {ECO:0000305}.
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DR EMBL; CP000099; AAZ70700.1; -; Genomic_DNA.
DR RefSeq; WP_011306746.1; NC_007355.1.
DR AlphaFoldDB; Q46BP2; -.
DR SMR; Q46BP2; -.
DR EnsemblBacteria; AAZ70700; AAZ70700; Mbar_A1758.
DR GeneID; 3625987; -.
DR KEGG; mba:Mbar_A1758; -.
DR eggNOG; arCOG03259; Archaea.
DR HOGENOM; CLU_014690_0_0_2; -.
DR OMA; IDYANAM; -.
DR OrthoDB; 4558at2157; -.
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; S-layer; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:22666082"
FT CHAIN 25..668
FT /note="Major S-layer protein"
FT /id="PRO_0000444299"
FT TRANSMEM 644..664
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 584..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..638
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 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 583
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 596
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 602
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 617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 635
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 668 AA; 73536 MW; 7398567AC77DA02C CRC64;
MKRFAAVTLA ALMLLTVFAS AASAADSVEI RGPVFNGSNI VEIVGDGITI DATQFAAFYY
DIDDNVTTET LSIKDVSGNS GNVIGEGGIV YSTKIQKVDY EYYKPSLGWD NYSLLGFFAE
KYIPLKSNSA DKLAKLVIDS DDKITLRTGE TLDIGQGYTL QAKQVDVDGE KVWLEFDRDG
EYVDDEIIEV GADDSTWDVE LDDIQDEDDV TVMRVHVNQV FQGAVDSIAQ IEGIWLIDYA
NAMTIESDDE FGDLDDVSIN GDTLNITNED TFTLTRDSTN ELAEGLSFKV ADTSSNVLRF
YLAKEFTDPG TYEVRGSVAS GEASWDASNF AGFYYDLDDN VETESLSVSE LNGNVIGEGG
LVYTTSIKKV DYDYENEDAG WDQYPIIGFF AEEYIPLKAN SADKLAKLVL DSDDKITLRT
GETFDLGEGY SIQAKQVDVD GEKVWLEFDK DGEYVDDEII EVGSNSDNTW DVELDDIEDE
DDVVVLKVHV NQVFRGAVDS IAQIEGIWLI DYANAMTIES DDEFGDLDDV SIQGDTLKIS
NEDTFTLTRD SDEDIGEGMY FKVADTPTSE LRYYPAIERI VGNETTSITK PDESGNETVS
DNETMPDNTS SETPDLNETD TPEEPTTTPE EPTDNETEPD ESNGSPGFGV VLGLAGLLGV
VYLVRRNN
