ENGB_ANAMF
ID ENGB_ANAMF Reviewed; 205 AA.
AC B9KIV1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Probable GTP-binding protein EngB {ECO:0000255|HAMAP-Rule:MF_00321};
GN Name=engB {ECO:0000255|HAMAP-Rule:MF_00321}; OrderedLocusNames=AMF_566;
OS Anaplasma marginale (strain Florida).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma.
OX NCBI_TaxID=320483;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Florida;
RX PubMed=19134224; DOI=10.1186/1471-2164-10-16;
RA Dark M.J., Herndon D.R., Kappmeyer L.S., Gonzales M.P., Nordeen E.,
RA Palmer G.H., Knowles D.P. Jr., Brayton K.A.;
RT "Conservation in the face of diversity: multistrain analysis of an
RT intracellular bacterium.";
RL BMC Genomics 10:16-16(2009).
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; CP001079; ACM49413.1; -; Genomic_DNA.
DR RefSeq; WP_010267811.1; NZ_AFMS01000114.1.
DR AlphaFoldDB; B9KIV1; -.
DR SMR; B9KIV1; -.
DR STRING; 320483.AMF_566; -.
DR EnsemblBacteria; ACM49413; ACM49413; AMF_566.
DR GeneID; 7398011; -.
DR KEGG; amf:AMF_566; -.
DR eggNOG; COG0218; Bacteria.
DR HOGENOM; CLU_033732_2_0_5; -.
DR OMA; LMMDIRH; -.
DR OrthoDB; 1746051at2; -.
DR Proteomes; UP000007307; 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..205
FT /note="Probable GTP-binding protein EngB"
FT /id="PRO_1000133042"
FT DOMAIN 21..196
FT /note="EngB-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 29..36
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 36
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 56..60
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 58
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 74..77
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 141..144
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 172..177
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
SQ SEQUENCE 205 AA; 22588 MW; 14644233ADA18E2E CRC64;
MLSKCRFVAG VQDKHSLPDF QVPEVAFAGR SNVGKSSLIN AVTKNKKGAR VSSNPGSTRQ
INFYLNEGAL ALVDLPGYGY SKASKESASS YMSLVEHYLL TREALHRLVL LIDSKVGLKE
VDMDFISWLE ERCIHYSLVL TKIDRLACTE FNDVLSAVQS RVKGCCMLLH PIIGTSSKSG
KGIKELVHEV SKCVKEWPGG RDVRA