ID A0LSM6_ACIC1 Unreviewed; 618 AA.
AC A0LSM6;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 24-JAN-2024, entry version 82.
DE SubName: Full=Peptidase S26B, signal peptidase {ECO:0000313|EMBL:ABK52436.1};
GN OrderedLocusNames=Acel_0663 {ECO:0000313|EMBL:ABK52436.1};
OS Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC Bacteria; Actinomycetota; Actinomycetes; Acidothermales; Acidothermaceae;
OC Acidothermus.
OX NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK52436.1, ECO:0000313|Proteomes:UP000008221};
RN [1] {ECO:0000313|EMBL:ABK52436.1, ECO:0000313|Proteomes:UP000008221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43068 / DSM 8971 / 11B
RC {ECO:0000313|Proteomes:UP000008221};
RX PubMed=19270083; DOI=10.1101/gr.084848.108;
RA Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT "Complete genome of the cellulolytic thermophile Acidothermus
RT cellulolyticus 11B provides insights into its ecophysiological and
RT evolutionary adaptations.";
RL Genome Res. 19:1033-1043(2009).
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DR EMBL; CP000481; ABK52436.1; -; Genomic_DNA.
DR RefSeq; WP_011719499.1; NC_008578.1.
DR AlphaFoldDB; A0LSM6; -.
DR STRING; 351607.Acel_0663; -.
DR KEGG; ace:Acel_0663; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_473045_0_0_11; -.
DR InParanoid; A0LSM6; -.
DR OrthoDB; 9802683at2; -.
DR Proteomes; UP000008221; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR CDD; cd06530; S26_SPase_I; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR019533; Peptidase_S26.
DR InterPro; IPR001733; Peptidase_S26B.
DR NCBIfam; TIGR02228; sigpep_I_arch; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008221};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 107..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 618 AA; 64368 MW; 64869BD4BC5B748A CRC64;
MAQDVAIRGD GPIAAGSTAR LVGGFLGRAW LWFLGGCLVI TVAPLIFGWR PYVVQTGSME
PRIHVGDVVL AAPVHDVNKL VGRVTVFYDP GRHEIVTHRV IGKNPDGTLV TKGDANPTPD
SAPLAPGNVR GMGRLLVRWL GLPVVWANHR DWLPLGGVAA SLALAGFLVA RDRDEDDVHA
DDAGAGEGGT GDGMDGGDGT DDGGDGTDGG PAGGGQSGGS DRSRQSAAPD YAPVTTAPGV
PAEYTQVPGD GGTGVVDMAV LAVEIPWPGH PLRRTDIGRP TGGRYVGRHR RPAHRRVVRS
VAAPAGAARR VSPVRRFAAR VAAVAVGLVA LVAPTSQAAF SAATQVTTNT WTAGVYNYTS
EVNALGPWLY WKLDDPITGR NPPAADSSGN GRPGVYSRPN SWTAQITGAL PDQTPNLAAL
SAGVTSTNNP SCIFTAQNGD GLAAPGPAAY TLVVWFRTAP GYANGGKLLG LESSRTGLSN
SNTGGRYDRM LYMDGAGHVW FGVWRTSIGQ AVAISSPSSY NDGNWHMAAA TMNATSGMTL
YVDGQPVATN PNTESETETT TSYWRAGCGN LAGWAVNWLG PNPPAAQTNY AFAGGLDEVA
VWLRALTATD IADLYFYR
//
