ID A0A0R0BJT8_9GAMM Unreviewed; 504 AA.
AC A0A0R0BJT8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=ATP-dependent protease {ECO:0000313|EMBL:KRG57597.1};
GN ORFNames=ABB25_09525 {ECO:0000313|EMBL:KRG57597.1};
OS Stenotrophomonas koreensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=266128 {ECO:0000313|EMBL:KRG57597.1, ECO:0000313|Proteomes:UP000051254};
RN [1] {ECO:0000313|EMBL:KRG57597.1, ECO:0000313|Proteomes:UP000051254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17805 {ECO:0000313|EMBL:KRG57597.1,
RC ECO:0000313|Proteomes:UP000051254};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-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:KRG57597.1}.
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; LDJH01000014; KRG57597.1; -; Genomic_DNA.
DR RefSeq; WP_057666202.1; NZ_LDJH01000014.1.
DR AlphaFoldDB; A0A0R0BJT8; -.
DR STRING; 266128.ABB25_09525; -.
DR PATRIC; fig|266128.3.peg.772; -.
DR OrthoDB; 9813147at2; -.
DR Proteomes; UP000051254; 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.
DR PROSITE; PS50051; MCM_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000313|EMBL:KRG57597.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:KRG57597.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051254}.
FT DOMAIN 290..385
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
SQ SEQUENCE 504 AA; 53393 MW; D1924D6C75A1F690 CRC64;
MSLALVHSRA RAGIDAPAVR VEVHLSGGLP AIQIVGLPEA AVRESRDRVR AALLCARFEW
PQRRITINLA PADLPKDGGR FDLPIALGIL AASGQIPLDA LAGHEFIGEL ALTGELRPVD
AVIPAVMAAA SSGHTLILPQ ANQAEAALVS QASTLVATTL LQVCAHLQGQ QSLPAAEPAV
QAGNLPNGPD MRDVRGQAQA RRALEVAAAG GHHLLLVGPP GCGKSMLASR LPGLLPALDE
QRALETAAIH SLGNTSKTLS AQWRRRPFRA PHHSASAVAL VGGGSHPRPG EISLAHNGVL
FLDELTQWQR GVLEVLREPL ETGSVTIARA ARSTTFPAQF QLVAAMNPCP CGWAGDISGR
CRCSSERITR YLGHLSGPLL DRIDLQVRIP RLPLELLAKP VAAAEDSACI AQRVANALQR
QWQRQGCANA QLDAAGTFAH CVLDGEQQNL LEQAAQRLQL SMRAVQRSLR VARTIADLND
QPSIDRAALA EALSYRQTAP EAAP
//