ID A0A0Q7A4K6_9BURK Unreviewed; 508 AA.
AC A0A0Q7A4K6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=ATP-dependent protease {ECO:0000313|EMBL:KQW35199.1};
GN ORFNames=ASC76_22735 {ECO:0000313|EMBL:KQW35199.1};
OS Rhizobacter sp. Root404.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736528 {ECO:0000313|EMBL:KQW35199.1, ECO:0000313|Proteomes:UP000051611};
RN [1] {ECO:0000313|EMBL:KQW35199.1, ECO:0000313|Proteomes:UP000051611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root404 {ECO:0000313|EMBL:KQW35199.1,
RC ECO:0000313|Proteomes:UP000051611};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW35199.1, ECO:0000313|Proteomes:UP000051611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root404 {ECO:0000313|EMBL:KQW35199.1,
RC ECO:0000313|Proteomes:UP000051611};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. ComM
CC subfamily. {ECO:0000256|ARBA:ARBA00006354}.
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:KQW35199.1}.
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DR EMBL; LMDS01000007; KQW35199.1; -; Genomic_DNA.
DR RefSeq; WP_056472411.1; NZ_LMDS01000007.1.
DR AlphaFoldDB; A0A0Q7A4K6; -.
DR STRING; 1736528.ASC76_22735; -.
DR OrthoDB; 9813147at2; -.
DR Proteomes; UP000051611; Unassembled WGS sequence.
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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:KQW35199.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:KQW35199.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051611}.
FT DOMAIN 219..400
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 508 AA; 52359 MW; DEFD2B3BDABF3533 CRC64;
MSLSVIHSRA LHALDAAEVT VEVHLANGLP SFTLVGLADT EVKEARERVR AAIQNSGLDF
PTNKRITVNL APADLPKESG RFDLPIALGI LAASGQIDPA RLGGFEFAGE LSLGGELRPV
RGALAMALAL QRHRAGPLRA LVLPQASARE AALVDGLAIH GAAHLLEVVA AMRPAGDAAP
APLPLVVASP QPTAAAGPDL RDVKGQAGAK RALEVAAAGS HSVLMVGSPG TGKSMLAQRF
AGLLPPLPHA QALESAAVLS LAGAFAPERW GRRVLRTPHH TASAAALAGG GSPPRPGEIS
LAHHGVLFLD ELPEFRRGAL EALREPLETG RIVISRAARQ AEFPARFQLL AAMNPCPCGH
LGSSLNSCRC APDAIARYQG KLSGPLLDRI DIQVEVPAVA PEALAAAPDG EPSAAIAARV
QVARARALAR QGCVNADLAG AALDAHTALD EATASILRSA AARLGWSARG FHRVLRVARS
VADLAASESI GIAHLAEAIQ YRRVLGAG
//
