ID Q832G1_ENTFA Unreviewed; 642 AA.
AC Q832G1;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Heparin-sulfate lyase N-terminal domain-containing protein {ECO:0000259|Pfam:PF16889};
GN OrderedLocusNames=EF_2268 {ECO:0000313|EMBL:AAO81996.1};
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185 {ECO:0000313|EMBL:AAO81996.1, ECO:0000313|Proteomes:UP000001415};
RN [1] {ECO:0000313|EMBL:AAO81996.1, ECO:0000313|Proteomes:UP000001415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583 {ECO:0000313|Proteomes:UP000001415};
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., Read T.D.,
RA Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L., Brinkac L., Beanan M., Daugherty S., DeBoy R.T.,
RA Durkin S., Kolonay J., Madupu R., Nelson W., Vamathevan J., Tran B.,
RA Upton J., Hansen T., Shetty J., Khouri H., Utterback T., Radune D.,
RA Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE016830; AAO81996.1; -; Genomic_DNA.
DR RefSeq; NP_815926.1; NC_004668.1.
DR RefSeq; WP_002359832.1; NZ_KE136528.1.
DR AlphaFoldDB; Q832G1; -.
DR STRING; 226185.EF_2268; -.
DR CAZy; PL12; Polysaccharide Lyase Family 12.
DR EnsemblBacteria; AAO81996; AAO81996; EF_2268.
DR KEGG; efa:EF2268; -.
DR PATRIC; fig|226185.45.peg.1263; -.
DR eggNOG; COG5434; Bacteria.
DR HOGENOM; CLU_013047_2_0_9; -.
DR Proteomes; UP000001415; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.70.98.70; -; 1.
DR Gene3D; 1.50.10.100; Chondroitin AC/alginate lyase; 1.
DR InterPro; IPR008929; Chondroitin_lyas.
DR InterPro; IPR012480; Hepar_II_III.
DR InterPro; IPR031680; Hepar_II_III_N.
DR PANTHER; PTHR39210; HEPARIN-SULFATE LYASE; 1.
DR PANTHER; PTHR39210:SF1; HEPARIN-SULFATE LYASE; 1.
DR Pfam; PF07940; Hepar_II_III; 1.
DR Pfam; PF16889; Hepar_II_III_N; 1.
DR SUPFAM; SSF48230; Chondroitin AC/alginate lyase; 1.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000001415};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 61..305
FT /note="Heparin-sulfate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16889"
SQ SEQUENCE 642 AA; 74824 MW; 163C7D83765DAC65 CRC64;
MNLQRIEDYQ LKFFQQDWLS EYLEQQSQFL KPLFERTSYL LKDQIIYNDA MDMEACSIPY
SLKEYAWNRY PDDDPEWLFM LSRQSFLVDL AQAYALTKKE RYLQKWHSLL IDFINDEGEP
NSTNRDVWRP LDVGIRVTNW MKSLTYIPIA DFRLLGIDDV LNNALLIHLD YLERSYIDKY
RLSNWGVLAI GGMAAIDLFL PELVTSKQRD LIWSRLAEQL DLQFYSDGIH WEQSPLYQHE
VLMTFVYLLQ ISEYLEVQLP LDLRMKLKTP IFSTHYLADN QDILNPINDS DHVNFHYVYD
IYRKLGFIFE PSMTANMARL WTGDLYEERI WETMKPKELF RGESSGLMAY KAEDIYFTLF
NGLHGSAHGH ASTGGFTLQL QGDDLFSDSG RYSYVNKSER LQLKECASHN TMFIAENPHT
LVSDTWGYDK LPTPLFQQIK ELSVGFFAEC GWLDKADQNP MIFERSFIYL KSINSVVIID
SFAGQKETEI TSTYNLAPSI NCQKEAHRFA LTTNKHKYTL LFAGGQTQQS VAKGSEIYNQ
LNEHPRLSNK FCYKTGKEIQ ATVISPLEDI QITPIKVSQT GENEQFCQAK GFRIIAGSEK
FDLFVMREDI VKGNKLLVSE YGQFFYGRLV LIDQKEAKIR IK
//
