ID A0A089LB89_9BACL Unreviewed; 576 AA.
AC A0A089LB89;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Fis family transcriptional regulator {ECO:0000313|EMBL:AIQ42094.1};
GN ORFNames=R50912_20100 {ECO:0000313|EMBL:AIQ42094.1};
OS Paenibacillus sp. FSL R5-0912.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1536771 {ECO:0000313|EMBL:AIQ42094.1, ECO:0000313|Proteomes:UP000029512};
RN [1] {ECO:0000313|EMBL:AIQ42094.1, ECO:0000313|Proteomes:UP000029512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-0912 {ECO:0000313|EMBL:AIQ42094.1,
RC ECO:0000313|Proteomes:UP000029512};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) 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; CP009282; AIQ42094.1; -; Genomic_DNA.
DR RefSeq; WP_042237171.1; NZ_CP009282.1.
DR AlphaFoldDB; A0A089LB89; -.
DR KEGG; paeq:R50912_20100; -.
DR HOGENOM; CLU_026145_1_1_9; -.
DR Proteomes; UP000029512; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0032508; P:DNA duplex unwinding; 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; IPR001208; MCM_dom.
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 PRINTS; PR01657; MCMFAMILY.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000029512}.
FT DOMAIN 274..460
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 165..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 576 AA; 62376 MW; DC789B932CE491C7 CRC64;
MYGKMHSACL YGIEGVMIGV EIDLANGLPQ TIIIGLPDSA VREAVERVRA AVKNCGYSYP
QQRVTINLAP ADLRKEGSAF DLAIALGILT TSGQLIMPDA GKMLLIGELA LDGSLRPVNG
VLSMVEAARR AGFQAVLVPP GNAAEAALIA GIRVYTSGHL RELSPSAAGV PASPSTVEPA
PGLEPRLPTE VADLEVQELF MPQTELPFPV SVSNEPSPRN RPPVQVLTLD HLGYQPEGNK
VLAPIREDYL MKEDYSDVIG QNHVKRALTI AAAGMHNIIL IGPPGTGKTM LIKRLPGILP
DLSDDESLEV MKIFSAAGKL RDSNGGLMRL RPFRSPHHTI SAAGLIGGGG IPKPGEVSLA
HRGILFLDEL PEFSRTVLEV LRQPLEDGVV TISRARASFT FPAQFLLACS MNPCMCGFLG
NGSSQQRCTC SPARIAQYRA KISGPLLDRM DMQVDVPRPK EVDRNVPALC TARMREEVLR
AQAIQAKRYQ HLPISWNSEL SGAALRRYAV LRHDESLLLN HILESLGLSM RAHDRIIKLA
RTIADLEGAE EIGSAHLAEA VQYRNLDRQV TAEEEY
//
