ID A0A0R2U6P1_9GAMM Unreviewed; 502 AA.
AC A0A0R2U6P1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 08-NOV-2023, entry version 20.
DE SubName: Full=ATP-dependent protease {ECO:0000313|EMBL:KRO95231.1};
GN ORFNames=ABS24_07805 {ECO:0000313|EMBL:KRO95231.1};
OS SAR92 bacterium BACL26 MAG-121220-bin70.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Porticoccaceae; SAR92 clade.
OX NCBI_TaxID=1655626 {ECO:0000313|EMBL:KRO95231.1, ECO:0000313|Proteomes:UP000051213};
RN [1] {ECO:0000313|EMBL:KRO95231.1, ECO:0000313|Proteomes:UP000051213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL26 MAG-121220-bin70 {ECO:0000313|EMBL:KRO95231.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-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:KRO95231.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LICA01000099; KRO95231.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2U6P1; -.
DR Proteomes; UP000051213; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:KRO95231.1};
KW Protease {ECO:0000313|EMBL:KRO95231.1}.
FT DOMAIN 209..388
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 502 AA; 55029 MW; EC5F3A586F0D7840 CRC64;
MSLAVIKSRA KLGIEAPIIS VEVHLSNGLP AFNIVGLPEA SVKESKDRVR SAIINSHFEF
PARRITVNLA PADIPKQGSR FDLAIAIGIL VASGQVPSDR VKDYEFIGEL ALTGDIRPVD
ALLPSAQRCS EADNQLIIAK ENAHEASLVE SLAVLPANHL LEVSAHLHGR ETIELWLRED
RVLTESTEEL SDIIGQQHAK RAMEIAATGG HHLLFYGPPG TGKTMLASRL AGILPPLSNQ
EALEVASIHS VAGKGLRQNI WLRPFRSPHH TASAAALVGG GGIPKPGEIS LAHHGVLFLD
ELPEFSRNVL EVLREPLESG QIMISRVNAQ TLYPAKFQLI AAMNPCPCGH LGSNRCVCPL
DQITRYQNKI SGPLLDRIDL QVQVSAITNH QLLSQETIAK GETNQQIQTR VCAARYLQIE
RQGKINADLS SQELREVCPL NKEQKSLMNQ AIDQFALSTR GFYRVLKVAR TLADLEKISY
PEIPHYQEAL SYRSTMDRRA SD
//