ID A0A193KE92_9VIBR Unreviewed; 643 AA.
AC A0A193KE92;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=A6E01_11890 {ECO:0000313|EMBL:ANO33867.1};
OS Vibrio breoganii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=553239 {ECO:0000313|EMBL:ANO33867.1, ECO:0000313|Proteomes:UP000092018};
RN [1] {ECO:0000313|EMBL:ANO33867.1, ECO:0000313|Proteomes:UP000092018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FF50 {ECO:0000313|EMBL:ANO33867.1,
RC ECO:0000313|Proteomes:UP000092018};
RA Hehemann J.-H., Arevalo P., Datta M.S., Yu X., Corzett C., Henschel A.,
RA Preheim S.P., Timberlake S., Alm E.J., Polz M.F.;
RT "Adaptive Radiation by Waves of Gene Transfer Leads to Fine-Scale Resource
RT Partitioning in Marine Microbes.";
RL Submitted (JUN-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}.
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DR EMBL; CP016177; ANO33867.1; -; Genomic_DNA.
DR RefSeq; WP_017027516.1; NZ_SYVS01000044.1.
DR AlphaFoldDB; A0A193KE92; -.
DR STRING; 553239.A6E01_11890; -.
DR KEGG; vbr:A6E01_11890; -.
DR eggNOG; COG0323; Bacteria.
DR OrthoDB; 9763467at2; -.
DR Proteomes; UP000092018; Chromosome 1.
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 213..331
FT /note="DNA mismatch repair protein S5"
FT /evidence="ECO:0000259|SMART:SM01340"
FT DOMAIN 465..601
FT /note="MutL C-terminal dimerisation"
FT /evidence="ECO:0000259|SMART:SM00853"
FT REGION 338..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 643 AA; 71683 MW; 0F23C8A1F7329105 CRC64;
MSEIKILPAR LANQIAAGEV VERPASVVKE LVENSIDAGA TRIDIDIEKG GSKLIRIRDN
GKGIIKDELQ LALSRHATSK ITTLDDLEAI MSLGFRGEAL ASISSVSRLT LTSRTATQEQ
AWAAYSEGRD MQVKLQPTAH PVGTSVEVLD LFFNTPARRK FLRTEKTEFT HIEELLKRIA
LSRFDVTLNL RHNGKLVKQY RAAKTERQVE QRIQSVCGKN FADNMLKVEL QHQDLKLYGW
ITTPAAARSQ GDLQYCYVNG RMMRDKLINH AIRQSYELAL RPEQFAAYVL FIEIDAHQVD
VNVHPAKHEV RFHQARLVHD FIYQALVDAL GQSQQLVSEE RRESAFATPH PQQSTASESE
QTTITPSPES KPISASPSQR EAQAMQQIPA YPNRADSAES SHGAPRSEGQ ARSSWGQNNT
SRTPKPQVSE QEAKVYQQLM TVEPSSAVET PSSVVAQPIT QLGKALTVVN ERFLLINTNA
GCGLLALSYA EILKLRGQLS VDQRQLVKQP LLIPLALRVR SEDIELLKQM QPMLERFAIQ
LMFKAGAKVM IMAVPQPLRH HNLQQLFSKL IDMLSGGQAL SFEQLSLWLA SQVAEQNKTY
TLSEAVQLLS DLEGASAQGL DLKDKKLIQL VDFSTQIKAL SHE
//
