ID A0A0S8FJJ9_9GAMM Unreviewed; 510 AA.
AC A0A0S8FJJ9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=ATP-dependent protease {ECO:0000313|EMBL:KPK60927.1};
GN ORFNames=AMJ59_04460 {ECO:0000313|EMBL:KPK60927.1};
OS Gammaproteobacteria bacterium SG8_31.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1703405 {ECO:0000313|EMBL:KPK60927.1, ECO:0000313|Proteomes:UP000051321};
RN [1] {ECO:0000313|EMBL:KPK60927.1, ECO:0000313|Proteomes:UP000051321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_31 {ECO:0000313|EMBL:KPK60927.1};
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:KPK60927.1}.
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DR EMBL; LJTI01000004; KPK60927.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8FJJ9; -.
DR PATRIC; fig|1703405.3.peg.1755; -.
DR Proteomes; UP000051321; 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:KPK60927.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:KPK60927.1}.
FT DOMAIN 212..394
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 490..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 510 AA; 54083 MW; BEA1A7422C8AEFB9 CRC64;
MGLAKVASRA YLGIAAPPVS VEVDLAGGLP ALSIVGLPEA TVRESKDRVR AALRNCGFDF
PPRRITVNLA PADLPKSGGR FDLPIALGVL AASGQLPSES LRGMEFIGEL SLDGRLRAVE
GSLSAAAAAS AERVTLIVPR GNMEEVLLVR DASLIAAGHL MSVWKHLAGH EELPPVVRGP
ASSCQSPPAN GDLAEVRGQP TARRALEIAA CGGHDMLMVG PPGTGKSMLA KRLPGLLPPL
ADAEALDVAL VTAARDGRFA AADWGRRPFR QPHHTATISA LVGGGSVPRP GEVSLAHRGV
LFMDELPEFP RGVLDALRQP LEDREVTISR ARGRLTFPAD FQLVAAMNPC PCGYFGDSFE
ACRCTPDAIR RYQGRISGPL MDRLDLRIDL VRPSAAILVD DAGEETSHTV AQRVLEARAR
QQRRGFLNAR IPPEMLVGLC QPTEAALALL CTSAERFHLS ARACHRVLRV ARTIADLAGR
SGIEAGDISE AVSRRPHASR AGRPRSAALS
//