ID A1UUD9_BARBK Unreviewed; 510 AA.
AC A1UUD9;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Mg chelatase homolog {ECO:0000313|EMBL:ABM45475.1};
GN OrderedLocusNames=BARBAKC583_1345 {ECO:0000313|EMBL:ABM45475.1};
OS Bartonella bacilliformis (strain ATCC 35685 / KC583 / Herrer 020/F12,63).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=360095 {ECO:0000313|EMBL:ABM45475.1, ECO:0000313|Proteomes:UP000000643};
RN [1] {ECO:0000313|EMBL:ABM45475.1, ECO:0000313|Proteomes:UP000000643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35685 / NCTC 12138 / KC583
RC {ECO:0000313|Proteomes:UP000000643};
RA Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S.,
RA Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R.,
RA Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J.,
RA Fraser-Ligget C., Seshadri R.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. ComM
CC subfamily. {ECO:0000256|ARBA:ARBA00006354}.
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DR EMBL; CP000524; ABM45475.1; -; Genomic_DNA.
DR RefSeq; WP_005768147.1; NC_008783.1.
DR AlphaFoldDB; A1UUD9; -.
DR STRING; 360095.BARBAKC583_1345; -.
DR GeneID; 72472738; -.
DR KEGG; bbk:BARBAKC583_1345; -.
DR PATRIC; fig|360095.6.peg.1318; -.
DR eggNOG; COG0606; Bacteria.
DR HOGENOM; CLU_026145_1_1_5; -.
DR OrthoDB; 9813147at2; -.
DR Proteomes; UP000000643; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR045006; CHLI-like.
DR InterPro; IPR004482; Mg_chelat-rel.
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 NCBIfam; TIGR00368; YifB family Mg chelatase-like AAA ATPase; 1.
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 SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000643}.
FT DOMAIN 209..391
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 510 AA; 55148 MW; C900413F60989798 CRC64;
MIACVTTVAF RGLEAIPVDV QVMISSGKIG MAIVGLADKA IAESRERVQA ALYACGLSMP
NKRVTINLAP ADLPKEGSHY DLPIAIGLML AMGVLPSEIV KNYLILGELS LDGSITAVNG
VLPTAMTALS LDKGLICPRQ CGPEAAWVNA DMDILAPDTL LTIINHFKGI QIQKRPQPRQ
YTIQTELPDL CEIKGQKTAK RALEVCAAGR HNLLFVGPPG AGKSMLAQCL PSILPPLDSR
ELLDVSLIAS IAGETAYNTL SLHCPFRAPH HSASMAAMIG GGLKGRPGEV SLAHNGILFL
DEFPEFAPQV LDSLRQPLES GECIIARVNH HISYPARIQL IAAMNPCRCG MAGEKGYVCA
KGTRCQTDYQ ARISGPLLDR IDLRIDVPAL TAMDLMQPEQ SEKSCNVAKR VARARAIQAK
RFAKMDLAHI RTNGDCPAKI IEQIATPDQN AAVLLRDVSE KMRLSARAYH RILKVARTIA
DLDEAQKLSR HHLAEAISYR LGNERLVALN
//
