ID E3E4C8_PAEPS Unreviewed; 814 AA.
AC E3E4C8;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Peptidase M28 {ECO:0000313|EMBL:ADO56668.1};
GN ORFNames=PPSC2_12660 {ECO:0000313|EMBL:ADO56668.1};
OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO56668.1, ECO:0000313|Proteomes:UP000006868};
RN [1] {ECO:0000313|EMBL:ADO56668.1, ECO:0000313|Proteomes:UP000006868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:ADO56668.1,
RC ECO:0000313|Proteomes:UP000006868};
RX PubMed=21037012; DOI=10.1128/JB.01234-10;
RA Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT activity.";
RL J. Bacteriol. 193:311-312(2011).
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall, S-layer
CC {ECO:0000256|ARBA:ARBA00004237}.
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DR EMBL; CP002213; ADO56668.1; -; Genomic_DNA.
DR RefSeq; WP_013371272.1; NC_014622.2.
DR AlphaFoldDB; E3E4C8; -.
DR KEGG; ppm:PPSC2_12660; -.
DR PATRIC; fig|886882.15.peg.2690; -.
DR eggNOG; COG2041; Bacteria.
DR eggNOG; COG3391; Bacteria.
DR eggNOG; COG4447; Bacteria.
DR HOGENOM; CLU_346769_0_0_9; -.
DR OrthoDB; 2480681at2; -.
DR Proteomes; UP000006868; Chromosome.
DR GO; GO:0030115; C:S-layer; IEA:UniProtKB-SubCell.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR032109; Big_3_5.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001119; SLH_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR43308; OUTER MEMBRANE PROTEIN ALPHA-RELATED; 1.
DR Pfam; PF16640; Big_3_5; 2.
DR Pfam; PF00395; SLH; 3.
DR SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 2.
DR PROSITE; PS51272; SLH; 3.
PE 4: Predicted;
KW Cell wall {ECO:0000256|ARBA:ARBA00022601};
KW Reference proteome {ECO:0000313|Proteomes:UP000006868};
KW S-layer {ECO:0000256|ARBA:ARBA00022601};
KW Secreted {ECO:0000256|ARBA:ARBA00022601}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..814
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003168536"
FT DOMAIN 619..682
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 685..748
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 749..810
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT REGION 529..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 814 AA; 86064 MW; 2E512E726B4A3AF2 CRC64;
MMLRTRTRRF AALIAAAVTF TTLVPGLPAS ADASPNPMEG IVLTKHERLG PEGFGTISYE
DGIFYLTGKN NRAYSDDGGS SWKKLYGNNA QMDTAGDGNG NFLTVVGSGG YIRWDTTTRA
LESFEKTIYY PGFKPSMPSV AYFKGSFYAA GYETATMPQL GRIFKLNDDG ESWEHIAVQG
PALENKRFNK IRTNGTTMVA VGEYGLIATS TDGVTWTQRE SGSSQHLVDV TVPADGSPIM
AVGMYNTITI SEDGGETWQA YGFKYDDPDI YSVTYARGYY VISNEYGKIL YSTDARNWSE
FNHGFGRIGI NAINIDLPGQ MVLVSGGGLV YSVSKATTST ALASSANPAS VEQEVVFTAT
VSKPSNSPVT AAPTGTVTFK NGESVLGSAP LTVGQATYSV SDLSIGTHQI TAVYSGDGAF
GTSASAPLGQ VVTDAVPKKS TTTTVTSTRN PSTVGQSVTI HATVTGPSGT PTGTLTFKDG
DTVLDAVPMT VGAATYSTTQ FMVGVHPITV TYSGDVQFEG STSATLHQTV NADDSGNSDN
GSGGSGGGSG GGSDPTTGTT PTAQPTTPEQ PDAQKPEGNG EIPQDPNDIF RSQVVRADSN
VIAGVQARTA EILENGGQFA SIQYNDLGDH WSIPNVEKLT KLGVIHGYPT GGFEPDAVIT
RAEFAAMIDR GFVDMASRKV EINEEDFAAF SDIEGHWSSD NLKQLVAVGV MTGYEDGTIR
PEKLITRQEM ALMITRVLNA YILNRDTSDV AFSDLDGAYG AEAIKKAAAL GIFTGKTKQR
FDPFAGATRA ESLQTIINTY TLSPAIKEAL DSLS
//