MUTL_BACSU
ID MUTL_BACSU Reviewed; 627 AA.
AC P49850;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=DNA mismatch repair protein MutL;
GN Name=mutL; OrderedLocusNames=BSU17050;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8760914; DOI=10.1099/13500872-142-8-2021;
RA Ginetti F., Perego M., Albertini A.M., Galizzi A.;
RT "Bacillus subtilis mutS mutL operon: identification, nucleotide sequence
RT and mutagenesis.";
RL Microbiology 142:2021-2029(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=12483591; DOI=10.2323/jgam.46.183;
RA Sasaki M., Yonemura Y., Kurusu Y.;
RT "Genetic analysis of Bacillus subtilis mutator genes.";
RL J. Gen. Appl. Microbiol. 46:183-187(2000).
RN [4]
RP POSSIBLE ROLE IN STATIONARY-PHASE-INDUCED MUTAGENESIS REPAIR.
RC STRAIN=168 / YB955;
RX PubMed=19011023; DOI=10.1128/jb.01210-08;
RA Vidales L.E., Cardenas L.C., Robleto E., Yasbin R.E., Pedraza-Reyes M.;
RT "Defects in the error prevention oxidized guanine system potentiate
RT stationary-phase mutagenesis in Bacillus subtilis.";
RL J. Bacteriol. 191:506-513(2009).
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 (By similarity). Overexpression of mutSL partially
CC suppresses the high spontaneous mutation frequency of a ytkD/mutM/mutY
CC triple disruption which lacks the system required to prevent damage by
CC oxidized guanine (8-oxo-dGTP). This suggests that MutSL also functions
CC to repair mismatches due to oxidative stress in both growing and
CC stationary phase cells. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene have an 80-fold increased
CC spontaneous mutation frequency. A double mutS/mutL and a triple
CC mutS/mutL/nth disruption has a 200 to 280-fold increased spontaneous
CC mutation frequency. {ECO:0000269|PubMed:12483591}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC {ECO:0000305}.
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DR EMBL; U27343; AAB19236.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13578.1; -; Genomic_DNA.
DR PIR; A69663; A69663.
DR RefSeq; NP_389587.1; NC_000964.3.
DR RefSeq; WP_003245099.1; NZ_JNCM01000035.1.
DR PDB; 3GAB; X-ray; 2.50 A; A/B/C/D=434-627.
DR PDB; 3KDG; X-ray; 2.00 A; A/B=434-627.
DR PDB; 3KDK; X-ray; 2.26 A; A/B=434-627.
DR PDBsum; 3GAB; -.
DR PDBsum; 3KDG; -.
DR PDBsum; 3KDK; -.
DR AlphaFoldDB; P49850; -.
DR SMR; P49850; -.
DR IntAct; P49850; 3.
DR STRING; 224308.BSU17050; -.
DR PaxDb; P49850; -.
DR PRIDE; P49850; -.
DR EnsemblBacteria; CAB13578; CAB13578; BSU_17050.
DR GeneID; 939455; -.
DR KEGG; bsu:BSU17050; -.
DR PATRIC; fig|224308.179.peg.1846; -.
DR eggNOG; COG0323; Bacteria.
DR InParanoid; P49850; -.
DR OMA; AHERIMY; -.
DR PhylomeDB; P49850; -.
DR BioCyc; BSUB:BSU17050-MON; -.
DR EvolutionaryTrace; P49850; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0032300; C:mismatch repair complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
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; IBA:GO_Central.
DR Gene3D; 3.30.1370.100; -; 1.
DR Gene3D; 3.30.1540.20; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.565.10; -; 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; IPR002099; DNA_mismatch_repair_N.
DR InterPro; IPR013507; DNA_mismatch_S5_2-like.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR038973; MutL/Mlh/Pms.
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_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR10073; PTHR10073; 2.
DR Pfam; PF01119; DNA_mis_repair; 1.
DR Pfam; PF08676; MutL_C; 1.
DR SMART; SM01340; DNA_mis_repair; 1.
DR SMART; SM00853; MutL_C; 1.
DR SUPFAM; SSF118116; SSF118116; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00585; mutl; 1.
DR PROSITE; PS00058; DNA_MISMATCH_REPAIR_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; Reference proteome.
FT CHAIN 1..627
FT /note="DNA mismatch repair protein MutL"
FT /id="PRO_0000177927"
FT REGION 354..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 440..445
FT /evidence="ECO:0007829|PDB:3KDG"
FT TURN 446..448
FT /evidence="ECO:0007829|PDB:3KDG"
FT STRAND 449..454
FT /evidence="ECO:0007829|PDB:3KDG"
FT STRAND 457..462
FT /evidence="ECO:0007829|PDB:3KDG"
FT HELIX 463..480
FT /evidence="ECO:0007829|PDB:3KDG"
FT STRAND 486..496
FT /evidence="ECO:0007829|PDB:3KDG"
FT HELIX 501..507
FT /evidence="ECO:0007829|PDB:3KDG"
FT HELIX 509..514
FT /evidence="ECO:0007829|PDB:3KDG"
FT STRAND 526..533
FT /evidence="ECO:0007829|PDB:3KDG"
FT HELIX 541..555
FT /evidence="ECO:0007829|PDB:3KDG"
FT HELIX 560..573
FT /evidence="ECO:0007829|PDB:3KDG"
FT HELIX 585..597
FT /evidence="ECO:0007829|PDB:3KDG"
FT STRAND 601..603
FT /evidence="ECO:0007829|PDB:3GAB"
FT STRAND 611..615
FT /evidence="ECO:0007829|PDB:3KDG"
FT HELIX 616..623
FT /evidence="ECO:0007829|PDB:3KDG"
SQ SEQUENCE 627 AA; 70431 MW; 068A0509CC265343 CRC64;
MAKVIQLSDE LSNKIAAGEV VERPASVVKE LVENAIDADS TVIEIDIEEA GLASIRVLDN
GEGMENEDCK RAFRRHATSK IKDENDLFRV RTLGFRGEAL PSIASVSHLE ITTSTGEGAG
TKLVLQGGNI ISESRSSSRK GTEIVVSNLF FNTPARLKYM KTVHTELGNI TDVVNRIALA
HPEVSIRLRH HGKNLLQTNG NGDVRHVLAA IYGTAVAKKM LPLHVSSLDF EVKGYIALPE
ITRASRNYMS SVVNGRYIKN FPLVKAVHEG YHTLLPIGRH PITFIEITMD PILVDVNVHP
SKLEVRLSKE TELHDLIRDG IKDVFKQQQL IPSAQVPKKS APAIKNEQQF ITFDEKPPEK
KVPEKSTAPS YSPMKLSSVV KEPVDAEEKL PPLQFDAPPI VDQEQTLEVS DVSAEQPETF
EQECHEEQPQ PASDRVPIMY PIGQMHGTYI LAQNENGLYI IDQHAAQERI KYEYFREKVG
EVEPEVQEMI VPLTFHYSTN EALIIEQHKQ ELESVGVFLE SFGSNSYIVR CHPAWFPKGE
EAELIEEIIQ QVLDSKNIDI KKLREEAAIM MSCKGSIKAN RHLRNDEIKA LLDDLRSTSD
PFTCPHGRPI IIHHSTYEME KMFKRVM
