ID B0SR77_LEPBP Unreviewed; 481 AA.
AC B0SR77;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Putative ATPase with chaperone activity {ECO:0000313|EMBL:ABZ97778.1};
GN OrderedLocusNames=LEPBI_I1671 {ECO:0000313|EMBL:ABZ97778.1};
OS Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ97778.1, ECO:0000313|Proteomes:UP000001847};
RN [1] {ECO:0000313|EMBL:ABZ97778.1, ECO:0000313|Proteomes:UP000001847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Patoc 1 / ATCC 23582 / Paris
RC {ECO:0000313|Proteomes:UP000001847};
RX PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL PLoS ONE 3:E1607-E1607(2008).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000786; ABZ97778.1; -; Genomic_DNA.
DR AlphaFoldDB; B0SR77; -.
DR STRING; 456481.LEPBI_I1671; -.
DR KEGG; lbi:LEPBI_I1671; -.
DR HOGENOM; CLU_026145_1_1_12; -.
DR OrthoDB; 9813147at2; -.
DR BioCyc; LBIF456481:LEPBI_RS08255-MONOMER; -.
DR Proteomes; UP000001847; Chromosome I.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR045006; CHLI-like.
DR InterPro; IPR025158; Mg_chelat-rel_C.
DR InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR PANTHER; PTHR32039:SF7; COMPETENCE PROTEIN COMM; 1.
DR PANTHER; PTHR32039; MAGNESIUM-CHELATASE SUBUNIT CHLI; 1.
DR Pfam; PF13541; ChlI; 1.
DR Pfam; PF01078; Mg_chelatase; 1.
DR Pfam; PF13335; Mg_chelatase_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001847}.
FT DOMAIN 197..380
FT /note="Magnesium chelatase ChlI-like catalytic"
FT /evidence="ECO:0000259|Pfam:PF01078"
FT DOMAIN 413..470
FT /note="Mg chelatase-related protein C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13335"
SQ SEQUENCE 481 AA; 55204 MW; 0DF8F39FAA503B74 CRC64;
MSPPKRAEVG SLMYEWNGTK EIQVEVGIRR GFPHFQILGN VPQEAKEARD RIRLALDASH
FDFPMETIII NVKPSHIQKK KVSLDLAMAV GILQATDQIK RPNRRIVYLG NLGLDGSLVG
GKELLPFLWQ KAEKKDQVYC LPDSLRNESL PDGEYYFLTD LQELESLSQK PPDVQKKTYT
MENPVWEEVY LDPFQMNAFQ GLLYALLGNH HSLLLGSPGV GKTMLHRLLE PLLPPKLTGE
QSNLGIWRAN GEFEVPTNKR PFRSPHHSTT EVGLLGGGLP YQPGEITRAE GGILFLDEAL
EFKDRILESL RMPMEDSYLE ITRLNEVTKM KTDFTLFLSS NPCPCGNYQS QNHCHCSLQK
IRLYLQKISG AFLDRITIFQ TLFVSNVERN IRLEEEKLKR IVNERFDFKK NRINSNEETK
KILQQLDISK ETKHLSLRKK KQIVSLARTI ADWNLSPRTK EVHIQEALDY SLGYQWIYSL
G
//
