ID F8FR35_PAEMK Unreviewed; 821 AA.
AC F8FR35;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Fibronectin type-III domain-containing protein {ECO:0000259|PROSITE:PS50853};
GN OrderedLocusNames=KNP414_01911 {ECO:0000313|EMBL:AEI40473.1};
OS Paenibacillus mucilaginosus (strain KNP414).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1036673 {ECO:0000313|EMBL:AEI40473.1, ECO:0000313|Proteomes:UP000006620};
RN [1] {ECO:0000313|Proteomes:UP000006620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KNP414 {ECO:0000313|Proteomes:UP000006620};
RA Wang J., Hu S., Hu X., Zhang B., Dong D., Zhang S., Zhao K., Wu D.;
RT "Complete genome sequence of Paenibacillus mucilaginosus KNP414.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEI40473.1, ECO:0000313|Proteomes:UP000006620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KNP414 {ECO:0000313|EMBL:AEI40473.1,
RC ECO:0000313|Proteomes:UP000006620};
RX PubMed=24158556;
RA Lu J.J., Wang J.F., Hu X.F.;
RT "Genome Sequence of Growth-Improving Paenibacillus mucilaginosus Strain
RT KNP414.";
RL Genome Announc. 1:e00881-13(2013).
CC -!- SIMILARITY: Belongs to the pectinesterase family.
CC {ECO:0000256|ARBA:ARBA00008891}.
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DR EMBL; CP002869; AEI40473.1; -; Genomic_DNA.
DR AlphaFoldDB; F8FR35; -.
DR KEGG; pms:KNP414_01911; -.
DR PATRIC; fig|1036673.3.peg.1707; -.
DR HOGENOM; CLU_344472_0_0_9; -.
DR Proteomes; UP000006620; Chromosome.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0030599; F:pectinesterase activity; IEA:InterPro.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR033131; Pectinesterase_Asp_AS.
DR InterPro; IPR000070; Pectinesterase_cat.
DR PANTHER; PTHR31321; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR PANTHER; PTHR31321:SF141; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR Pfam; PF01095; Pectinesterase; 1.
DR SMART; SM00060; FN3; 4.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 3: Inferred from homology;
KW Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023085}.
FT DOMAIN 1..47
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 50..141
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 232..327
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 29..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 477
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 821 AA; 86652 MW; F6B8511DBDDB0203 CRC64;
MASNVTAATY IDESVQNGTT YYYVVTASGT TGESGPSNQV TVSPSEDAVK PEAPAGLTAG
ARSTQVDLSW QPAERANTYT VKRSTNPEGP FTVIASGLGS TSYRDGGLDN GTEYSYVVSA
VGVGGEGAGS APVAVTPSRQ LSTPVVTVQS LPSGALVQWG PVDGASSYLV KRADQYGGPY
EVLAESVTGV TYTDSGLING KPYYYKVTAV DGTTHSLDSS SAGVRPSAQD GTPAPPPGLT
AEPGDSSIRL NWMEVPEAAS YTVKRSDTAE GPYTTAASGL SNPSFTDSGL VNGKNYYYLV
SAVNEAGEGG TSVPVREVPA QVLTVAADGS AQYTKVQDAI QAVPDNSATP TIIKIKNGTY
REKLDLPSAK INVRMIGESR EGTVLIYGDA ASTLDANGNP LGTSNSYSFR VQARDFTAEH
LTIQNDAGDD AGQAVALYAN GDRMAFRDVS LRGYQDTLYS NNGRQYFTDS YIEGDVDFIF
GNASAVFENS IIHSLSSGYV TAASTAEGKT GYVFLNSRIT AEPGLTGTVA LGRPWRAYSN
VKYVNSYMDD HIKPVGWDNW GRTENESTAQ YGEYASYGPG ADPKARFRWS KQLTTEEAAL
LTPADILGGS DGWNPFAAVP LVDGSRELAA LTVNDAPVPD FSPATTQYRI ELQDPRILPV
VTAAVYSDTS LVSVKQAASV PGTAEVHIQA RDGGERTYTI QFAAADHQAP TLKLEVDQPV
LQADDHRMVS VHASVYASDE GTGVASIRLL SITSSEPEND QGDGNTAVDI QGAEYGTADY
DFELRAERSG PGSGRIYTIT YEAVDFAGNR IQASTTVTIL H
//
