CSG_METTL
ID CSG_METTL Reviewed; 559 AA.
AC Q8X235;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 23-FEB-2022, entry version 38.
DE RecName: Full=S-layer protein {ECO:0000303|PubMed:12382110};
DE AltName: Full=Cell surface glycoprotein {ECO:0000305};
DE Flags: Precursor;
GN Name=slmt1 {ECO:0000303|PubMed:12382110};
OS Methanothermococcus thermolithotrophicus (Methanococcus
OS thermolithotrophicus).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanothermococcus.
OX NCBI_TaxID=2186;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 29-45, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 35097 / DSM 2095 / JCM 10549 / OCM 138 / SN-1;
RX PubMed=12382110; DOI=10.1007/s00792-001-0264-1;
RA Akca E., Claus H., Schultz N., Karbach G., Schlott B., Debaerdemaeker T.,
RA Declercq J.P., Konig H.;
RT "Genes and derived amino acid sequences of S-layer proteins from
RT mesophilic, thermophilic, and extremely thermophilic methanococci.";
RL Extremophiles 6:351-358(2002).
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:12382110}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall, S-layer
CC {ECO:0000269|PubMed:12382110}.
CC -!- SIMILARITY: Belongs to the Mj S-layer protein family. {ECO:0000305}.
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DR EMBL; AJ308554; CAC83952.2; -; Genomic_DNA.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0030115; C:S-layer; IEA:UniProtKB-SubCell.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR InterPro; IPR022651; S_layer_C.
DR InterPro; IPR006454; S_layer_MJ.
DR InterPro; IPR022650; S_layer_N.
DR Pfam; PF05124; S_layer_C; 1.
DR Pfam; PF05123; S_layer_N; 1.
DR TIGRFAMs; TIGR01564; S_layer_MJ; 1.
PE 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation; Direct protein sequencing;
KW Glycoprotein; S-layer; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:12382110"
FT CHAIN 29..559
FT /note="S-layer protein"
FT /id="PRO_0000444301"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 559 AA; 59232 MW; 8F61979E633C6EB6 CRC64;
MAMSLKKIGA IAVGGAMVAS ALASGVMAAT TSGDVAGFMK NAIKEDGTPN VDIVVGSGAA
VMDVVSAADV AAKIGSMAYK TGVVEDRSAV VKVSAKAESD DVNIFTLNAT NEDIALVAAA
DSDYAKGFIN GSDQLKVTDQ LASGSIQDVN DADFNATSLG DVSTMLKVPD IDPSDWYSND
DDAGEVVFTR IVYDSDKLSI DEDQILYASI AYKNDEDVFN DNNTVTLKPG MRIPFLGEEY
AVVKIDDEDD IIYLGKEAKD GVLKEGEXFA VGNGYEVKIA SILKSGDTST EYSVNVQILK
DGKVVKEKTD TVGGSSSAQL KLAYKDVGVV VNDAWEDIAG TTGYAEVLIT KDTKALELGE
EYIPDWEAYA ALNNSDKLEI KKDITESDKA NIIGIALKYV GDKKKKLGDR DEVDIANYLK
LVFDDEDKND VLKVKFLMDE SKEVTLDIGQ KATVLNAEVR LKDILADAQQ SVKLTAPIAK
LDSEVSLDTA DKNLILVGGP VVNALTKELV DAGKVAIDNT SPATLAVVEG AANGNDVLVV
AGGDREATRE AAKALLEMI
