MUTL_VIBCH
ID MUTL_VIBCH Reviewed; 653 AA.
AC Q9KV13;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=DNA mismatch repair protein MutL;
GN Name=mutL; OrderedLocusNames=VC_0345;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC {ECO:0000305}.
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; AE003852; AAF93518.1; -; Genomic_DNA.
DR PIR; A82334; A82334.
DR RefSeq; NP_229999.1; NC_002505.1.
DR RefSeq; WP_000155485.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KV13; -.
DR SMR; Q9KV13; -.
DR STRING; 243277.VC_0345; -.
DR DNASU; 2615058; -.
DR EnsemblBacteria; AAF93518; AAF93518; VC_0345.
DR KEGG; vch:VC_0345; -.
DR PATRIC; fig|243277.26.peg.322; -.
DR eggNOG; COG0323; Bacteria.
DR HOGENOM; CLU_004131_5_1_6; -.
DR OMA; ATQEQAW; -.
DR BioCyc; VCHO:VC0345-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
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 3: Inferred from homology;
KW DNA damage; DNA repair; Reference proteome.
FT CHAIN 1..653
FT /note="DNA mismatch repair protein MutL"
FT /id="PRO_0000177989"
FT REGION 375..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 653 AA; 72631 MW; 5D970C21A17C66FF CRC64;
MTIRILPARL ANQIAAGEVV ERPASVVKEL VENSLDAGAT RIDIDLEKGG AKLIRIRDNG
SGIDKDELGL ALSRHATSKI HTLDDLEAIM SLGFRGEALA SISSVSRLTL TSRTVAQEEA
WSAYSEGRDM AVKLQPAAHP VGTTVEVLDL FFNTPARRKF LRTEKTEFTH IDELLKRIAL
SRFDVSFTLR HNGKIVRQYR AATTLPQQEK RLAAVCGNPF VQHMLRIELE HQGLKLHGWI
TTPEGARQQS DLQYCYVNGR MMRDKLINHA IRQSYETSLR VDQFATYVLF IELDPHQVDV
NVHPAKHEVR FHQARLVHDF IYQALSSALV QGAQVMAPTI NEGAFHLPHC AEEVNPPVVP
MIDTTQQERV WQAVQNTPDY PRKAPRDNDR DESDNPQVRE RAVSNPWVAS PKTASTGKER
YGSASVSKKE AAVYQTLMQT PDLSDEEPST ASTIVSSIEA VKANIAIEKL GKAIQVVAGQ
YLLMSSPQGC VLISLYQAQQ LKLRGLLNAQ HGALKAQPLL VPLALKLNES EWQVAQRHSS
ALLQLGIELK SRTNHSIMVM AVPQPLRQQN LQQLLPDLLS YAASCSESQA LSHQALADWL
TQRIVVEKRD YTLAEAIGLI AELEQLWQGN LPLQDPHFIT LVDFSASITA LHS