ID   T2B1_HERAU              Reviewed;         274 AA.
AC   P25257;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   28-JUN-2023, entry version 66.
DE   RecName: Full=Type II restriction enzyme HgiBI {ECO:0000303|PubMed:12654995};
DE            Short=R.HgiBI {ECO:0000305|PubMed:2062638};
DE            EC=3.1.21.4 {ECO:0000269|PubMed:7607523};
DE   AltName: Full=Endonuclease HgiBI;
DE   AltName: Full=Type-2 restriction enzyme HgiBI;
GN   Name=hgiBIR {ECO:0000303|PubMed:7607523};
OS   Herpetosiphon aurantiacus (Herpetosiphon giganteus).
OC   Bacteria; Chloroflexota; Chloroflexia; Herpetosiphonales;
OC   Herpetosiphonaceae; Herpetosiphon.
OX   NCBI_TaxID=65;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=HPG5;
RX   PubMed=2062638; DOI=10.1093/nar/19.12.3207;
RA   Duesterhoeft A., Erdmann D., Kroeger M.;
RT   "Isolation and genetic structure of the AvaII isoschizomeric restriction-
RT   modification system HgiBI from Herpetosiphon giganteus Hpg5: M.HgiBI
RT   reveals high homology to M.BanI.";
RL   Nucleic Acids Res. 19:3207-3211(1991).
RN   [2]
RP   DISCUSSION OF SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
RP   SER-176.
RX   PubMed=7607523; DOI=10.1016/0378-1119(94)00779-r;
RA   Kroeger M., Blum E., Deppe E., Duesterhoeft A., Erdmann D., Kilz S.,
RA   Meyer-Rogge S., Moestl D.;
RT   "Organization and gene expression within restriction-modification systems
RT   of Herpetosiphon giganteus.";
RL   Gene 157:43-47(1995).
RN   [3]
RP   NOMENCLATURE, AND SUBTYPE.
RX   PubMed=12654995; DOI=10.1093/nar/gkg274;
RA   Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA   Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA   Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA   Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA   Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA   Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA   Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA   Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA   Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT   "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT   endonucleases and their genes.";
RL   Nucleic Acids Res. 31:1805-1812(2003).
CC   -!- FUNCTION: A P subtype restriction enzyme that recognizes the double-
CC       stranded sequence 5'-GGWCC-3' and cleaves after G-1 (PubMed:7607523,
CC       PubMed:12654995). This system is less active than isoschizomeric
CC       RM.HgiEI (PubMed:7607523). {ECO:0000269|PubMed:7607523,
CC       ECO:0000303|PubMed:12654995}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of DNA to give specific double-
CC         stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4;
CC         Evidence={ECO:0000269|PubMed:7607523};
CC   -!- SIMILARITY: Belongs to the TdeIII type II restriction endonuclease
CC       family. {ECO:0000305}.
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DR   EMBL; X55137; CAA38928.1; -; Genomic_DNA.
DR   PIR; S22308; S22308.
DR   AlphaFoldDB; P25257; -.
DR   REBASE; 1098; HgiBI.
DR   PRO; PR:P25257; -.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   InterPro; IPR019045; Restrct_endonuc_II_TdeIII.
DR   Pfam; PF09520; RE_TdeIII; 1.
PE   1: Evidence at protein level;
KW   Endonuclease; Hydrolase; Nuclease; Restriction system.
FT   CHAIN           1..274
FT                   /note="Type II restriction enzyme HgiBI"
FT                   /id="PRO_0000077310"
FT   MUTAGEN         176
FT                   /note="S->D: Increased specific activity."
FT                   /evidence="ECO:0000269|PubMed:7607523"
SQ   SEQUENCE   274 AA;  31189 MW;  301A50CD604A56FC CRC64;
     MAINPITRNK IKDYLNSFIQ QQLSVYSQRS LREFQDVDSY PSSLSKDGDL KPFHASLIPA
     SIMRLNRFER SLSTGLGSTF EECTRLIALD HHAVALRNYD IQAALDQAQW AAIDQLISTI
     DRGLKHQTPS LNQMLEQIQS IPLTGILETH IVRADLYIQR HDGSELFFEI KSPKPSKGQC
     LEVMQRLLRI YTIKQQSAVP VKAFYAMAYN PWGISRASYR SSITKKYTDF SNAVVIGQEF
     WSLIGEPSTY TELLEIYHEV GLAKSAEITQ KLLQ
//