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Database: UniProt
Entry: A0A268E217_9BACI
LinkDB: A0A268E217_9BACI
Original site: A0A268E217_9BACI 
ID   A0A268E217_9BACI        Unreviewed;       394 AA.
AC   A0A268E217;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 11.
DE   SubName: Full=Cobalamin biosynthesis protein CobW {ECO:0000313|EMBL:PAD67161.1};
GN   ORFNames=CHH83_20255 {ECO:0000313|EMBL:PAD67161.1};
OS   Bacillus sp. 7586-K.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2021690 {ECO:0000313|EMBL:PAD67161.1, ECO:0000313|Proteomes:UP000216230};
RN   [1] {ECO:0000313|EMBL:PAD67161.1, ECO:0000313|Proteomes:UP000216230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7586-K {ECO:0000313|EMBL:PAD67161.1,
RC   ECO:0000313|Proteomes:UP000216230};
RA   Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA   Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT   "Isolation and whole genome analysis of endospore-forming bacteria from
RT   heroin.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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:PAD67161.1}.
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DR   EMBL; NPCL01000105; PAD67161.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A268E217; -.
DR   OrthoDB; 9808822at2; -.
DR   Proteomes; UP000216230; 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; PTHR43603; COBW DOMAIN-CONTAINING PROTEIN DDB_G0274527; 1.
DR   PANTHER; PTHR43603:SF3; METAL CHAPERONE YCIC-RELATED; 1.
DR   Pfam; PF02492; cobW; 1.
DR   Pfam; PF07683; CobW_C; 1.
DR   SMART; SM00833; CobW_C; 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:UP000216230}.
FT   DOMAIN          256..371
FT                   /note="CobW C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00833"
SQ   SEQUENCE   394 AA;  44981 MW;  D1691C0831EB9FAC CRC64;
     MKRKVPVTVL SGYLGSGKTT LLNHVLQNRE NLKVAVIVND MSEVNIDATM VKKGGFSRTD
     EKLVEMQNGC ICCTLREDLI VEVERLVKAG DIDYILIESS GISEPIPVAQ TFTYIDENLK
     INLPEYCELD TMVTVVDANR FWHDFASGES LLDRKQGNDE TDTREIVDLL IDQIEFANVL
     VLNKIDLVDR ESIEELKLVL QKLNPEARII ESAYSVVALS CILNTGLFDF ERASQAAGWI
     KELNEEHTPE TEEYGVSSFV YRRRKPFHPE RWLRWLENWP VEVVRAKGFF WLATRNNMTG
     LLSQAGPSII FQGAGEWIAA ASKQEQAKIL EEDPELLERW DEVYGDRMNE LVLIGIDLNK
     EQIEAALDEC LLTDEEMIQD WSKFHDPLPP FIVE
//
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