ID MUTL_BACCN Reviewed; 649 AA.
AC A7GR98;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=DNA mismatch repair protein MutL {ECO:0000255|HAMAP-Rule:MF_00149};
GN Name=mutL {ECO:0000255|HAMAP-Rule:MF_00149}; OrderedLocusNames=Bcer98_2420;
OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315749;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98;
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
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:0000255|HAMAP-Rule:MF_00149}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC {ECO:0000255|HAMAP-Rule:MF_00149}.
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DR EMBL; CP000764; ABS22656.1; -; Genomic_DNA.
DR RefSeq; WP_012094855.1; NC_009674.1.
DR AlphaFoldDB; A7GR98; -.
DR SMR; A7GR98; -.
DR STRING; 315749.Bcer98_2420; -.
DR GeneID; 56417960; -.
DR KEGG; bcy:Bcer98_2420; -.
DR eggNOG; COG0323; Bacteria.
DR HOGENOM; CLU_004131_4_1_9; -.
DR OrthoDB; 9763467at2; -.
DR Proteomes; UP000002300; 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; 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; DNA repair.
FT CHAIN 1..649
FT /note="DNA mismatch repair protein MutL"
FT /id="PRO_1000076688"
FT REGION 339..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 649 AA; 74339 MW; 4609C381303640A6 CRC64;
MGKIRKLDEQ LSNLIAAGEV VERPASVVKE LVENSIDANS TSIEIHLEEA GLSKIRIIDN
GDGIAEEDCI VAFERHATSK IKDENDLFRI RTLGFRGEAL PSIASVSELE LVTSTGDAPG
THLIIKGGEI IKQEKTASRK GTDITVQNLF FNTPARLKYM KTIHTELGNI TDIVYRIAMS
HPEVSLKLFH NTKKLLHTSG NGDVRQVLAA IYSIQVAKKL IPIEAESLDF TIRGYVTLPE
VTRASRNYMS TIVNGRYVRN YVLMKAIQQG YHTLLPVGRY PIGFLSIEMD PMLVDVNVHP
AKLEVRFSKE QELLQFIEQT LQDAFKKVQL IPDAGVTTKK KTKDESVQEQ FHFEHTKPKE
PSMPNIVLPT GMDEAQEEES AEKPSVAPQL WQQPKQEWQP PQSLVREEES WQSTSKPLIE
EKAAHNEQEW DHHEEEFELE ELDELQNIEE IEMNGNDLPP LYPIGQMHGT YIFAQNDKGL
YMIDQHAAQE RINYEYFRDK VGQVTQEVQE LLVPYRIDLS LNEFLRVEEQ LEELKKVGLF
LEQFGHQSFI VRSHPIWFPK GKETEIIDEM MQQVVKLKKV DIKKLREEAA IMMSCKASIK
ANQYLTNDQI FALLEELRTT SNPYTCPHGR PIIIHHSTYE LEKMFKRVM
//
