ID V9WA95_9BACL Unreviewed; 204 AA.
AC V9WA95;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Probable GTP-binding protein EngB {ECO:0000256|HAMAP-Rule:MF_00321};
GN Name=engB {ECO:0000256|HAMAP-Rule:MF_00321,
GN ECO:0000313|EMBL:AHD06640.1};
GN ORFNames=ERIC2_c28560 {ECO:0000313|EMBL:AHD06640.1};
OS Paenibacillus larvae subsp. larvae DSM 25430.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=697284 {ECO:0000313|EMBL:AHD06640.1, ECO:0000313|Proteomes:UP000029431};
RN [1] {ECO:0000313|EMBL:AHD06640.1, ECO:0000313|Proteomes:UP000029431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25430 {ECO:0000313|EMBL:AHD06640.1,
RC ECO:0000313|Proteomes:UP000029431};
RX PubMed=24599066;
RA Djukic M., Brzuszkiewicz E., Funfhaus A., Voss J., Gollnow K., Poppinga L.,
RA Liesegang H., Garcia-Gonzalez E., Genersch E., Daniel R.;
RT "How to Kill the Honey Bee Larva: Genomic Potential and Virulence
RT Mechanisms of Paenibacillus larvae.";
RL PLoS ONE 9:E90914-E90914(2014).
CC -!- FUNCTION: Necessary for normal cell division and for the maintenance of
CC normal septation. {ECO:0000256|HAMAP-Rule:MF_00321}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. EngB GTPase family. {ECO:0000256|ARBA:ARBA00009638,
CC ECO:0000256|HAMAP-Rule:MF_00321}.
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DR EMBL; CP003355; AHD06640.1; -; Genomic_DNA.
DR RefSeq; WP_024094786.1; NZ_CP019652.1.
DR AlphaFoldDB; V9WA95; -.
DR KEGG; plv:ERIC2_c28560; -.
DR PATRIC; fig|697284.3.peg.2706; -.
DR eggNOG; COG0218; Bacteria.
DR HOGENOM; CLU_033732_3_0_9; -.
DR Proteomes; UP000029431; 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; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR03598; GTPase_YsxC; 1.
DR PANTHER; PTHR11649:SF13; ENGB-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11649; MSS1/TRME-RELATED GTP-BINDING PROTEIN; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51706; G_ENGB; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_00321};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_00321};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00321}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00321}; Reference proteome {ECO:0000313|Proteomes:UP000029431};
KW Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00321}.
FT DOMAIN 22..195
FT /note="EngB-type G"
FT /evidence="ECO:0000259|PROSITE:PS51706"
SQ SEQUENCE 204 AA; 23389 MW; CF3A449ECED1C2E8 CRC64;
MKVNEAQFVI SAVGPSQYPT DALPEIALAG RSNVGKSSLI NRLINRKNLA RTSSQPGKTQ
TLNYYLINQD LYFVDLPGYG YAKVSKAKRA EWGKFIENYL LKREPLKLVL QLIDLRHPPT
KDDQAMYAWL KHHKLPVCVV TTKADKIPKG KWQKHCKVIK ETLEFEKSDH MIVFSSETGQ
GKEELWSFIE NKIGWEQQET AIKE
//
