ID A0A0S8H4G0_9BACT Unreviewed; 517 AA.
AC A0A0S8H4G0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 08-NOV-2023, entry version 20.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=AMS25_10915 {ECO:0000313|EMBL:KPK79952.1};
OS Gemmatimonas sp. SM23_52.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=1703359 {ECO:0000313|EMBL:KPK79952.1, ECO:0000313|Proteomes:UP000051975};
RN [1] {ECO:0000313|EMBL:KPK79952.1, ECO:0000313|Proteomes:UP000051975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_52 {ECO:0000313|EMBL:KPK79952.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK79952.1}.
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DR EMBL; LJUM01000067; KPK79952.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8H4G0; -.
DR PATRIC; fig|1703359.3.peg.54; -.
DR Proteomes; UP000051975; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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;
FT DOMAIN 213..396
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 517 AA; 54887 MW; 479D3222963D0E33 CRC64;
MLACARTAAF LGIDAYVVVV EVDAAAGLPA MATVGLAQSA VKEGKERVLS AIQNSGFEVP
PRKITINLAP ADIKKEGSHF DLPIACGVLA ATGQLSGDSL ERFALAGELG LDGALRPIRG
ALPMAQALAA SGLPGLIIPA PNLPEASIID GLDVRGASTL GEVAGFLQGR VELRREPLDP
AGLLHRRSGT AVDLKDVRGQ GYAKRALEVA AAGAHNILLV GPPGGGKTML ARRLPSILPK
LSLAEAIEVT RVHSVAGLLA PDQALVSERP FRAPHHTVSD AGLVGGGAIP RPGEASLAHH
GVLFLDELTE FRRNVLEVLR QPLEDGHVTI GRAAGTLTYP ARFVLAAAMN PCPCGHLGDR
RKRCRCTPRM IQRYRAKISG PLLDRIDLHI EVPPVATPDL LGADDSEDSA DVAQRVERAR
HLQLARFRGR DGLFANGQMG PRDVHRYCRT DETSLSLLRA AMARFSLSAR SYHRVLKLAR
TIADLEASEI IRAAHVAEAI QYRGLDRNIL DLAGACP
//
