ID   ENGB_NEIMF              Reviewed;         209 AA.
AC   A1KS92;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Probable GTP-binding protein EngB {ECO:0000255|HAMAP-Rule:MF_00321};
GN   Name=engB {ECO:0000255|HAMAP-Rule:MF_00321}; OrderedLocusNames=NMC0415;
OS   Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS   15464 / FAM18).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=272831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700532 / DSM 15464 / FAM18;
RX   PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA   Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA   Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA   Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA   Quail M.A., Achtman M., Barrell B.G., Saunders N.J., Parkhill J.;
RT   "Meningococcal genetic variation mechanisms viewed through comparative
RT   analysis of serogroup C strain FAM18.";
RL   PLoS Genet. 3:230-240(2007).
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; AM421808; CAM09722.1; -; Genomic_DNA.
DR   RefSeq; WP_002217904.1; NC_008767.1.
DR   AlphaFoldDB; A1KS92; -.
DR   SMR; A1KS92; -.
DR   EnsemblBacteria; CAM09722; CAM09722; NMC0415.
DR   KEGG; nmc:NMC0415; -.
DR   HOGENOM; CLU_033732_1_0_4; -.
DR   OMA; LMMDIRH; -.
DR   Proteomes; UP000002286; 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; Septation.
FT   CHAIN           1..209
FT                   /note="Probable GTP-binding protein EngB"
FT                   /id="PRO_1000005833"
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"
SQ   SEQUENCE   209 AA;  23562 MW;  5FBCC4A20809E970 CRC64;
     MNLFQNAKFF TTVNHLKDLP DTPLEIAFVG RSNAGKSSAI NTLTNHVRLA YVSKTPGRTQ
     HINFFELQNG NFMVDLPGYG YAQVPEAVRA HWVNLLGDYL QQRKQLIGLV LIMDARHPLK
     ELDIRMLDFF HTTGRPVHIL LSKADKLSKN EQIKTLSQVK KLLKPYSDRQ NISVQLFSSL
     KKQGIDEANR TVGSWFDAAD AAASSPKEN