ENGB_ACHLI
ID ENGB_ACHLI Reviewed; 191 AA.
AC A9NFM5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Probable GTP-binding protein EngB {ECO:0000255|HAMAP-Rule:MF_00321};
GN Name=engB {ECO:0000255|HAMAP-Rule:MF_00321}; OrderedLocusNames=ACL_0537;
OS Acholeplasma laidlawii (strain PG-8A).
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Acholeplasma.
OX NCBI_TaxID=441768;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG-8A;
RX PubMed=21784942; DOI=10.1128/jb.05059-11;
RA Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A.,
RA Vereshchagin V.V., Kostrjukova E.S., Kovaleva G.Y., Kazanov M.D.,
RA Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Demina I.A.,
RA Serebryakova M.V., Galyamina M.A., Vtyurin N.N., Rogov S.I., Alexeev D.G.,
RA Ladygina V.G., Govorun V.M.;
RT "Complete genome and proteome of Acholeplasma laidlawii.";
RL J. Bacteriol. 193:4943-4953(2011).
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; CP000896; ABX81155.1; -; Genomic_DNA.
DR RefSeq; WP_012242486.1; NC_010163.1.
DR AlphaFoldDB; A9NFM5; -.
DR SMR; A9NFM5; -.
DR STRING; 441768.ACL_0537; -.
DR EnsemblBacteria; ABX81155; ABX81155; ACL_0537.
DR KEGG; acl:ACL_0537; -.
DR eggNOG; COG0218; Bacteria.
DR HOGENOM; CLU_033732_3_2_14; -.
DR OMA; LMMDIRH; -.
DR OrthoDB; 1746051at2; -.
DR Proteomes; UP000008558; 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 3: Inferred from homology;
KW Cell cycle; Cell division; GTP-binding; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Septation.
FT CHAIN 1..191
FT /note="Probable GTP-binding protein EngB"
FT /id="PRO_1000115949"
FT DOMAIN 22..191
FT /note="EngB-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 30..37
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
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 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
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 BINDING 75..78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 142..145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 172..174
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
SQ SEQUENCE 191 AA; 21929 MW; DCDC645F04663339 CRC64;
MMIKQAEFIT SAVSITDLPK DDFDHFLILG RSNVGKSSLI NAITNRKKLA RVSQTPGKTI
TLNLYLLNQS LYLVDAPGYG YAKRSKTQTL TFMRMINEYI QLNGHLKKII LLVDFNIGPT
QDDLDMYIEL QAFDVDIIVV TTKYDKVKSS HRLKQEKVIR SKFFEGQKIY FTSSETKFGI
DKLINEEFSN E