ENGB_PYRHO
ID ENGB_PYRHO Reviewed; 216 AA.
AC O57939;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Probable GTP-binding protein EngB {ECO:0000255|HAMAP-Rule:MF_00321};
GN Name=engB {ECO:0000255|HAMAP-Rule:MF_00321}; OrderedLocusNames=PH0200;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
CC -!- FUNCTION: Necessary for normal cell division and for the maintenance of
CC normal septation. {ECO:0000255|HAMAP-Rule:MF_00321}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00321};
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. EngB GTPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00321}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA29269.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BA000001; BAA29269.1; ALT_FRAME; Genomic_DNA.
DR PIR; F71242; F71242.
DR PDB; 2CXX; X-ray; 1.70 A; A/B/C=27-216.
DR PDBsum; 2CXX; -.
DR AlphaFoldDB; O57939; -.
DR SMR; O57939; -.
DR STRING; 70601.3256586; -.
DR EnsemblBacteria; BAA29269; BAA29269; BAA29269.
DR KEGG; pho:PH0200; -.
DR eggNOG; arCOG00355; Archaea.
DR EvolutionaryTrace; O57939; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR CDD; cd01876; YihA_EngB; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00321; GTPase_EngB; 1.
DR InterPro; IPR030393; G_ENGB_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR019987; GTP-bd_ribosome_bio_YsxC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51706; G_ENGB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; GTP-binding; Magnesium;
KW Metal-binding; Nucleotide-binding; Septation.
FT CHAIN 1..216
FT /note="Probable GTP-binding protein EngB"
FT /id="PRO_0000157814"
FT DOMAIN 26..210
FT /note="EngB-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 34..41
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 41
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 59..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 61
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 76..79
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 156..159
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 189..191
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:2CXX"
FT HELIX 40..48
FT /evidence="ECO:0007829|PDB:2CXX"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:2CXX"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:2CXX"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:2CXX"
FT HELIX 88..105
FT /evidence="ECO:0007829|PDB:2CXX"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:2CXX"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:2CXX"
FT HELIX 120..130
FT /evidence="ECO:0007829|PDB:2CXX"
FT HELIX 136..146
FT /evidence="ECO:0007829|PDB:2CXX"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:2CXX"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:2CXX"
FT HELIX 164..175
FT /evidence="ECO:0007829|PDB:2CXX"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:2CXX"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:2CXX"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:2CXX"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:2CXX"
FT HELIX 197..210
FT /evidence="ECO:0007829|PDB:2CXX"
SQ SEQUENCE 216 AA; 25051 MW; 33B80F8B1A0E92E7 CRC64;
MKLSTADSIF FFLPYEFINP IILLIPMATI IFAGRSNVGK STLIYRLTGK KVRRGKRPGV
TRKIIEIEWK NHKIIDMPGF GFMMGLPKEV QERIKDEIVH FIEDNAKNID VAVLVVDGKA
APEIIKRWEK RGEIPIDVEF YQFLRELDIP TIVAVNKLDK IKNVQEVINF LAEKFEVPLS
EIDKVFIPIS AKFGDNIERL KNRIFEVIRE RQGRRV
