ID A0A1M3PGV3_9PROT Unreviewed; 599 AA.
AC A0A1M3PGV3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=DNA mismatch repair protein MutL {ECO:0000256|ARBA:ARBA00021975, ECO:0000256|HAMAP-Rule:MF_00149};
GN Name=mutL {ECO:0000256|HAMAP-Rule:MF_00149};
GN ORFNames=BGP12_17970 {ECO:0000313|EMBL:OJY65734.1};
OS Rhodospirillales bacterium 70-18.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales.
OX NCBI_TaxID=1895826 {ECO:0000313|EMBL:OJY65734.1, ECO:0000313|Proteomes:UP000184399};
RN [1] {ECO:0000313|EMBL:OJY65734.1, ECO:0000313|Proteomes:UP000184399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-18 {ECO:0000313|EMBL:OJY65734.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This protein is involved in the repair of mismatches in DNA.
CC It is required for dam-dependent methyl-directed DNA mismatch repair.
CC May act as a 'molecular matchmaker', a protein that promotes the
CC formation of a stable complex between two or more DNA-binding proteins
CC in an ATP-dependent manner without itself being part of a final
CC effector complex. {ECO:0000256|HAMAP-Rule:MF_00149}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC {ECO:0000256|ARBA:ARBA00006082, ECO:0000256|HAMAP-Rule:MF_00149}.
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:OJY65734.1}.
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DR EMBL; MKWE01000051; OJY65734.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3PGV3; -.
DR STRING; 1895826.BGP12_17970; -.
DR Proteomes; UP000184399; Unassembled WGS sequence.
DR GO; GO:0032300; C:mismatch repair complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR GO; GO:0006298; P:mismatch repair; IEA:UniProtKB-UniRule.
DR CDD; cd16926; HATPase_MutL-MLH-PMS-like; 1.
DR CDD; cd00782; MutL_Trans; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.1540.20; MutL, C-terminal domain, dimerisation subdomain; 1.
DR Gene3D; 3.30.1370.100; MutL, C-terminal domain, regulatory subdomain; 1.
DR HAMAP; MF_00149; DNA_mis_repair; 1.
DR InterPro; IPR014762; DNA_mismatch_repair_CS.
DR InterPro; IPR020667; DNA_mismatch_repair_MutL.
DR InterPro; IPR013507; DNA_mismatch_S5_2-like.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR002099; MutL/Mlh/PMS.
DR InterPro; IPR038973; MutL/Mlh/Pms-like.
DR InterPro; IPR014790; MutL_C.
DR InterPro; IPR042120; MutL_C_dimsub.
DR InterPro; IPR042121; MutL_C_regsub.
DR InterPro; IPR037198; MutL_C_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00585; mutl; 1.
DR PANTHER; PTHR10073; DNA MISMATCH REPAIR PROTEIN MLH, PMS, MUTL; 1.
DR PANTHER; PTHR10073:SF12; DNA MISMATCH REPAIR PROTEIN MLH1; 1.
DR Pfam; PF01119; DNA_mis_repair; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF08676; MutL_C; 1.
DR SMART; SM01340; DNA_mis_repair; 1.
DR SMART; SM00853; MutL_C; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF118116; DNA mismatch repair protein MutL; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00058; DNA_MISMATCH_REPAIR_1; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00149};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00149}.
FT DOMAIN 209..327
FT /note="DNA mismatch repair protein S5"
FT /evidence="ECO:0000259|SMART:SM01340"
FT DOMAIN 412..556
FT /note="MutL C-terminal dimerisation"
FT /evidence="ECO:0000259|SMART:SM00853"
FT REGION 345..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 599 AA; 62567 MW; 6F7DB980ED42F794 CRC64;
MRAGRIRMLP EATVNRIAAG EVIERPAAAA RELVENALDA GATRIAVAID GGGIDRIEVV
DDGSGMTDEE LALAVQRHAT SKLADDTLVH ILTLGFRGEA LPSIGAAARL SITSRPAGAD
HAASIRVEGG AVGEPAPAAG PPGTRVVVRD LFFATPARRK FLKTPRAEAD ATEAAIRRLA
LAAPGVAFRL ESDGRVAFDL PAQDRQARVA ALLGPDAAAA LLEVDGGRGD MRLTGFIGAP
TVSRATAAAQ ALVVNGRPVT DPLLRTAVRV AYRDVIAYGR HPVVALFLDL PPEELDVNVH
PAKAEVRFRD AAGVRGLVIA TLARTLAGGA ILGTAPSVQV RLDADRPMGR PQSSRPGLSL
HAAPRPHAPQ GFAEALLPME AAPAARVLPA PDRFHGPFSA AAPATAYPLG APVAQVLDTY
VIAVAADGSL VLVDQHAAHE RLTHEDIRAQ LLDGGVRSQK LLLPGVVDLP PADAQRLLAR
AGELAQLGLE IEAFGPGAVL VRALPAVLGA PDPGPLLRDL ADEFAEMDEA TALDARLDAV
VARLACHGSI RAGRRLAGPE MDALLRRMEA TPRAATCSHG RPTFLKLSRA EIERMFGRR
//