ENGB_NEIG2
ID ENGB_NEIG2 Reviewed; 209 AA.
AC B4RQ29;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Probable GTP-binding protein EngB {ECO:0000255|HAMAP-Rule:MF_00321};
GN Name=engB {ECO:0000255|HAMAP-Rule:MF_00321}; OrderedLocusNames=NGK_0143;
OS Neisseria gonorrhoeae (strain NCCP11945).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=521006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCCP11945;
RX PubMed=18586945; DOI=10.1128/jb.00566-08;
RA Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.;
RT "Complete genome sequence of Neisseria gonorrhoeae NCCP11945.";
RL J. Bacteriol. 190:6035-6036(2008).
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}.
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DR EMBL; CP001050; ACF28841.1; -; Genomic_DNA.
DR RefSeq; WP_003687358.1; NC_011035.1.
DR PDB; 5UCV; X-ray; 1.80 A; A/B=1-209.
DR PDBsum; 5UCV; -.
DR AlphaFoldDB; B4RQ29; -.
DR SMR; B4RQ29; -.
DR EnsemblBacteria; ACF28841; ACF28841; NGK_0143.
DR GeneID; 66752366; -.
DR KEGG; ngk:NGK_0143; -.
DR HOGENOM; CLU_033732_1_0_4; -.
DR OMA; LMMDIRH; -.
DR OrthoDB; 1746051at2; -.
DR Proteomes; UP000002564; 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 Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03598; GTPase_YsxC; 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..209
FT /note="Probable GTP-binding protein EngB"
FT /id="PRO_1000115989"
FT DOMAIN 22..198
FT /note="EngB-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 37
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 59
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT STRAND 8..15
FT /evidence="ECO:0007829|PDB:5UCV"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:5UCV"
FT STRAND 23..31
FT /evidence="ECO:0007829|PDB:5UCV"
FT HELIX 36..44
FT /evidence="ECO:0007829|PDB:5UCV"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:5UCV"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:5UCV"
FT HELIX 86..102
FT /evidence="ECO:0007829|PDB:5UCV"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:5UCV"
FT HELIX 121..131
FT /evidence="ECO:0007829|PDB:5UCV"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:5UCV"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:5UCV"
FT HELIX 149..163
FT /evidence="ECO:0007829|PDB:5UCV"
FT HELIX 164..168
FT /evidence="ECO:0007829|PDB:5UCV"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:5UCV"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:5UCV"
FT HELIX 185..198
FT /evidence="ECO:0007829|PDB:5UCV"
SQ SEQUENCE 209 AA; 23600 MW; 79742D484A0A1ABF CRC64;
MNLFQNAKFF TTVNHLKDLP DTPLEIAFVG RSNAGKSSAI NTLTNHVRLA YVSKTPGRTQ
HINFFELQNG NFMVDLPGYG YAQVPEAVRA HWVNLLGDYL RHRKQLIGLV LIMDARHPLK
ELDIRMLDFF HTTGRPVHIL LSKADKLSKN EQIKTLSQVK KLLKPYSDRQ NISVQLFSSL
KKQGIDEANR TVGSWFDAAD AAASSPEEN
