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Database: UniProt
Entry: K6C394_9BACI
LinkDB: K6C394_9BACI
Original site: K6C394_9BACI 
ID   K6C394_9BACI            Unreviewed;       302 AA.
AC   K6C394;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Cobalamin synthesis protein/P47K family protein {ECO:0000313|EMBL:EKN65600.1};
GN   ORFNames=BABA_19591 {ECO:0000313|EMBL:EKN65600.1};
OS   Neobacillus bataviensis LMG 21833.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX   NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN65600.1, ECO:0000313|Proteomes:UP000006316};
RN   [1] {ECO:0000313|EMBL:EKN65600.1, ECO:0000313|Proteomes:UP000006316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX   PubMed=23087684;
RA   Heylen K., Keltjens J.;
RT   "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT   reduction in Bacillus.";
RL   Front. Microbiol. 3:371-371(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000256|ARBA:ARBA00001702};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000256|ARBA:ARBA00001702};
CC   -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. ZNG1
CC       subfamily. {ECO:0000256|ARBA:ARBA00034320}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKN65600.1}.
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DR   EMBL; AJLS01000130; EKN65600.1; -; Genomic_DNA.
DR   RefSeq; WP_007086911.1; NZ_AJLS01000130.1.
DR   AlphaFoldDB; K6C394; -.
DR   STRING; 1117379.BABA_19591; -.
DR   PATRIC; fig|1117379.3.peg.4060; -.
DR   eggNOG; COG0523; Bacteria.
DR   OrthoDB; 9808822at2; -.
DR   Proteomes; UP000006316; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd03112; CobW-like; 1.
DR   Gene3D; 3.30.1220.10; CobW-like, C-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR036627; CobW-likC_sf.
DR   InterPro; IPR011629; CobW-like_C.
DR   InterPro; IPR003495; CobW/HypB/UreG_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13748:SF62; COBW DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR13748; COBW-RELATED; 1.
DR   Pfam; PF02492; cobW; 1.
DR   Pfam; PF07683; CobW_C; 1.
DR   SMART; SM00833; CobW_C; 1.
DR   SUPFAM; SSF90002; Hypothetical protein YjiA, C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006316}.
FT   DOMAIN          214..299
FT                   /note="CobW C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00833"
SQ   SEQUENCE   302 AA;  34461 MW;  CB62DF81BA75CF2D CRC64;
     MKKAEVYILS GFLGSGKTTL LKRLLEDERD AGRRVAVMMN ELGKVSIDSD AINDDVALKE
     LLGGCICCSI QDKLEAQLQG LLQDEQPDVI YIETTGAAHP VEVLDAILSP LFADELIIKG
     IITTVDGTRW NGRKSLSPQL QQLILEQVRH ADFIIINKMD DLKEMEQANI TFEIQGINPK
     ARCLLTNFSQ VSIAQLRHLS VSFEKESQKI DLNLTTFVYQ FKIAINQTKF EEFLRELPDT
     IYRIKGYLKF DYSKQPFLFQ FSYGMPLYMK EEMNLPLNLV FIGENINWND IQEQLASLEK
     IN
//
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