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Database: UniProt
Entry: G8PIF0_PSEUV
LinkDB: G8PIF0_PSEUV
Original site: G8PIF0_PSEUV 
ID   G8PIF0_PSEUV            Unreviewed;       552 AA.
AC   G8PIF0;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Heparinase II/III family protein {ECO:0000313|EMBL:AEV34739.1};
GN   OrderedLocusNames=PSE_0227 {ECO:0000313|EMBL:AEV34739.1};
OS   Pseudovibrio sp. (strain FO-BEG1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Stappiaceae; Pseudovibrio.
OX   NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV34739.1, ECO:0000313|Proteomes:UP000005634};
RN   [1] {ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA   Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile and symbiotically
RT   interacting bacteria.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEV34739.1, ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV34739.1,
RC   ECO:0000313|Proteomes:UP000005634};
RX   PubMed=23601235; DOI=10.1111/1462-2920.12123;
RA   Bondarev V., Richter M., Romano S., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile bacteria adapted
RT   for symbiosis.";
RL   Environ. Microbiol. 15:2095-2113(2013).
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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DR   EMBL; CP003147; AEV34739.1; -; Genomic_DNA.
DR   RefSeq; WP_014283186.1; NC_016642.1.
DR   AlphaFoldDB; G8PIF0; -.
DR   STRING; 911045.PSE_0227; -.
DR   KEGG; psf:PSE_0227; -.
DR   eggNOG; COG5360; Bacteria.
DR   HOGENOM; CLU_025266_0_0_5; -.
DR   Proteomes; UP000005634; 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   PANTHER; PTHR39210; HEPARIN-SULFATE LYASE; 1.
DR   PANTHER; PTHR39210:SF1; HEPARIN-SULFATE LYASE; 1.
DR   Pfam; PF07940; Hepar_II_III; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
SQ   SEQUENCE   552 AA;  61038 MW;  C4533A4E89414E39 CRC64;
     MAQNSLNWAR GGSMFRMFSF GSAPSRLLIA PQDLRTADAT NAADIYAGRF LFAGHLVEVG
     GQSPFDVEPP NLQWAKALHG FSWLRHLRAA ETNMAQQNAR ALVEDWIKTC GRWHDIGWKQ
     EVVARRVLSW MAQSPLLLTG CEADFYRAFM RSLFRQVRFL RKTMNKAPDG LPRLTVAMAN
     ACATVSMDGQ GRHIKQALKR LDQELKRQIL PDGGHISRHP GAIIEILVDL LPIRQALVMQ
     GQTVSPVMME SIDRMMPMIR FFRHGDGSFA HFNGMASTPG DVVATILAYD DARGTPPVSA
     PHSGYQRLTG GDSLVVMDVG APPPTRFSNS THAGCLSFEF SSKRNRIVVN CGVSTREQVA
     WKMVARSTAA HSTAGIGDAS SCRFLTSSRF DKVLGNPVLS GPKDVSAERQ DTDLSDRVIA
     SHDGYVDRYG INHERDLTLS RDGTVLDGID RFKPTSDKAE EETVTIRFHL HPQVTCTMLP
     MGDAAVLQCA DGEAWEFTAE GLEFSVEESI YLSDVFGHRQ TQQIVISLSV KEAQSVTWML
     RKTASAKGRR KT
//
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