ID C9Y179_CROTZ Unreviewed; 634 AA.
AC C9Y179;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
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 ECO:0000313|EMBL:CBA33989.1};
GN OrderedLocusNames=Ctu_36900 {ECO:0000313|EMBL:CBA33989.1};
OS Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=693216 {ECO:0000313|EMBL:CBA33989.1, ECO:0000313|Proteomes:UP000002069};
RN [1] {ECO:0000313|Proteomes:UP000002069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18703 / CCUG 55852 / LMG 23827 / z3032
RC {ECO:0000313|Proteomes:UP000002069};
RX PubMed=21037008; DOI=10.1128/JB.01162-10;
RA Stephan R., Lehner A., Tischler P., Rattei T.;
RT "Complete genome sequence of Cronobacter turicensis LMG 23827, a food-borne
RT pathogen causing deaths in neonates.";
RL J. Bacteriol. 193:309-310(2011).
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}.
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DR EMBL; FN543093; CBA33989.1; -; Genomic_DNA.
DR AlphaFoldDB; C9Y179; -.
DR KEGG; ctu:CTU_36900; -.
DR PATRIC; fig|693216.3.peg.3492; -.
DR HOGENOM; CLU_004131_5_1_6; -.
DR Proteomes; UP000002069; Chromosome.
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; cd03482; MutL_Trans_MutL; 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 212..331
FT /note="DNA mismatch repair protein S5"
FT /evidence="ECO:0000259|SMART:SM01340"
FT DOMAIN 458..591
FT /note="MutL C-terminal dimerisation"
FT /evidence="ECO:0000259|SMART:SM00853"
FT REGION 356..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 634 AA; 69396 MW; EEE208AC320E1D6E CRC64;
MPIQVLPPQL ANQIAAGEVV ERPASVVKEL VENSLDAGAT RIDIDIERGG AKLIRIRDNG
GGIKKDELAL ALARHATSKI ASLDDLEAII SLGFRGEALA SISSVSRLTL TSRTADQHEA
WQAYAEGRDM DVTVKPAAHP VGTTLEVLDL FYNTPARRKF MRTEKTEFTH IDEVVRRIAL
ARFDVTINLS HNGKMMRQYR AVQGNAPRER RLGSICGPAF LEQALAIEWQ HGDLALHGWV
AEPKATTAAL AEIQYCYVNG RMMRDRLINH AIRQACEDKL GIDQQPAYVL YLEIDPHQVD
VNVHPAKHEV RFHQSRLVHD FIYQGVVSVL QQQAANPLSL NEPAEDAPRW HPENRVAAGK
NQFADPAPRE RERATIRESD APRHASGGAS AGTGRSGASN GGWPNATPGY QKQQGALYKQ
LLETPAVTSP VAPATAATRE TAPPAPALEG HSHSFGRVLT LVSENVALLE RDGKLMLLAL
SVAERCLKQA QLLPRDEAPC AQPLLIPVRL KISGDEREVM TRAQPQLARL GIEIVLDGHH
VTIRAVPLPL RQQNLQILIP ELIGYLAQQP NAYDAAVAGW LARHLVIAQP WSVAQAIATL
AELERLCPQM VKTPPGGLLQ LIDLQPAMNA LTHE
//
