ID A0A1D8P5W5_9FLAO Unreviewed; 609 AA.
AC A0A1D8P5W5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=DNA mismatch repair protein MutL {ECO:0000256|HAMAP-Rule:MF_00149};
GN Name=mutL {ECO:0000256|HAMAP-Rule:MF_00149};
GN ORFNames=LPB138_04440 {ECO:0000313|EMBL:AOW19978.1};
OS Urechidicola croceus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Urechidicola.
OX NCBI_TaxID=1850246 {ECO:0000313|EMBL:AOW19978.1, ECO:0000313|Proteomes:UP000176050};
RN [1] {ECO:0000313|EMBL:AOW19978.1, ECO:0000313|Proteomes:UP000176050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0138 {ECO:0000313|EMBL:AOW19978.1,
RC ECO:0000313|Proteomes:UP000176050};
RA Kim E., Yi H.;
RT "Lutibacter sp. LPB0138, isolated from marine gastropod.";
RL Submitted (OCT-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; CP017478; AOW19978.1; -; Genomic_DNA.
DR RefSeq; WP_070236117.1; NZ_CP017478.1.
DR AlphaFoldDB; A0A1D8P5W5; -.
DR STRING; 1850246.LPB138_04440; -.
DR KEGG; lul:LPB138_04440; -.
DR OrthoDB; 9763467at2; -.
DR Proteomes; UP000176050; 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 {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}; Reference proteome {ECO:0000313|Proteomes:UP000176050}.
FT DOMAIN 209..327
FT /note="DNA mismatch repair protein S5"
FT /evidence="ECO:0000259|SMART:SM01340"
FT DOMAIN 425..567
FT /note="MutL C-terminal dimerisation"
FT /evidence="ECO:0000259|SMART:SM00853"
SQ SEQUENCE 609 AA; 69035 MW; 3566E7FA54A97EED CRC64;
MTDIIQLLPD HVANQIAAGE VVQRPASVVK ELLENAIDAG ATSIKLLIKD AGKSLIQVID
NGKGMSETDA RFCFERHATS KIRTAEDLFN LQTKGFRGEA LASIAAIAHV ELKTKQALQE
LGTHIKIEGS SIVSQDLITT PKGTSIAVKN LFYNIPARRN FLKSNQVETR HIIDEFQRVA
LVHSTIEFSM YHNDNEVYRL NSCNLRQRIV SILGKKTNEK LVPINEKTDV LTLSGFVSKP
EFSKKKRGEQ FFFVNDRFIK NSYLHHALVS AFDGLLAGGY HPSYFLYLTV PPSTIDINIH
PTKTEIKFDN EKILYAIIRS TVKHSLGQYN ITPALDFNRD STLDVPYDYK DVKSSKEPKI
TINPNFNPFK AETQKTIQFP FKRDSKPQEW ESLYTDIEAI DVKNIEVESE IINNQLFENE
ISIAKTHQVH RKYIVSTIKS GIIFINQNLA HQRILYEEYL ESITVKEAMS QQLLFPLEIG
FSKDDIQLIK EIQLDLESTG FLFDKIEKET IVVKGIPTTI SESQVTIIIE QLLDDIKHEI
PETSFSQLDV MAKSLAKSLA IKSGSKLTIK EQESIVEQLF LCKEPNHSPF GKPTFISMEL
EEIDKKFGI
//
