ID A0A140NML5_PROSM Unreviewed; 672 AA.
AC A0A140NML5;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=UvrABC system protein B {ECO:0000256|ARBA:ARBA00029504, ECO:0000256|HAMAP-Rule:MF_00204};
DE Short=Protein UvrB {ECO:0000256|HAMAP-Rule:MF_00204};
DE AltName: Full=Excinuclease ABC subunit B {ECO:0000256|HAMAP-Rule:MF_00204};
GN Name=uvrB {ECO:0000256|HAMAP-Rule:MF_00204};
GN OrderedLocusNames=S70_15945 {ECO:0000313|EMBL:AFH95004.1};
OS Providencia stuartii (strain MRSN 2154).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=1157951 {ECO:0000313|EMBL:AFH95004.1, ECO:0000313|Proteomes:UP000005012};
RN [1] {ECO:0000313|EMBL:AFH95004.1, ECO:0000313|Proteomes:UP000005012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSN 2154 {ECO:0000313|EMBL:AFH95004.1,
RC ECO:0000313|Proteomes:UP000005012};
RX PubMed=22740665; DOI=10.1128/JB.00615-12;
RA Clifford R.J., Hang J., Riley M.C., Onmus-Leone F., Kuschner R.A.,
RA Lesho E.P., Waterman P.E.;
RT "Complete Genome Sequence of Providencia stuartii Clinical Isolate MRSN
RT 2154.";
RL J. Bacteriol. 194:3736-3737(2012).
RN [2] {ECO:0000313|Proteomes:UP000005012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSN 2154 {ECO:0000313|Proteomes:UP000005012};
RA Clifford R.J., Hang J., Riley M.C., Onmus-Leone F., Kuschner R.A.,
RA Lesho E.P., Waterman P.E.;
RT "Complete genome sequence of Providencia stuartii clinical isolate MRSN
RT 2154.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The UvrABC repair system catalyzes the recognition and
CC processing of DNA lesions. A damage recognition complex composed of 2
CC UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of
CC the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps
CC around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB
CC and probably causes local melting of the DNA helix, facilitating
CC insertion of UvrB beta-hairpin between the DNA strands. Then UvrB
CC probes one DNA strand for the presence of a lesion. If a lesion is
CC found the UvrA subunits dissociate and the UvrB-DNA preincision complex
CC is formed. This complex is subsequently bound by UvrC and the second
CC UvrB is released. If no lesion is found, the DNA wraps around the other
CC UvrB subunit that will check the other stand for damage.
CC {ECO:0000256|HAMAP-Rule:MF_00204}.
CC -!- SUBUNIT: Forms a heterotetramer with UvrA during the search for
CC lesions. Interacts with UvrC in an incision complex.
CC {ECO:0000256|ARBA:ARBA00026033, ECO:0000256|HAMAP-Rule:MF_00204,
CC ECO:0000256|RuleBase:RU003587}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00204, ECO:0000256|RuleBase:RU003587}.
CC -!- DOMAIN: The beta-hairpin motif is involved in DNA binding.
CC {ECO:0000256|HAMAP-Rule:MF_00204}.
CC -!- SIMILARITY: Belongs to the UvrB family. {ECO:0000256|ARBA:ARBA00008533,
CC ECO:0000256|HAMAP-Rule:MF_00204, ECO:0000256|RuleBase:RU003587}.
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DR EMBL; CP003488; AFH95004.1; -; Genomic_DNA.
DR RefSeq; WP_004917833.1; NC_017731.1.
DR AlphaFoldDB; A0A140NML5; -.
DR KEGG; psi:S70_15945; -.
DR PATRIC; fig|1157951.4.peg.3206; -.
DR HOGENOM; CLU_009621_2_1_6; -.
DR OrthoDB; 9806651at2; -.
DR Proteomes; UP000005012; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR CDD; cd17916; DEXHc_UvrB; 1.
DR CDD; cd18790; SF2_C_UvrB; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR Gene3D; 4.10.860.10; UVR domain; 1.
DR HAMAP; MF_00204; UvrB; 1.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001943; UVR_dom.
DR InterPro; IPR036876; UVR_dom_sf.
DR InterPro; IPR004807; UvrB.
DR InterPro; IPR041471; UvrB_inter.
DR InterPro; IPR024759; UvrB_YAD/RRR_dom.
DR NCBIfam; TIGR00631; uvrb; 1.
DR PANTHER; PTHR24029; UVRABC SYSTEM PROTEIN B; 1.
DR PANTHER; PTHR24029:SF0; UVRABC SYSTEM PROTEIN B; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF04851; ResIII; 1.
DR Pfam; PF02151; UVR; 1.
DR Pfam; PF12344; UvrB; 1.
DR Pfam; PF17757; UvrB_inter; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF46600; C-terminal UvrC-binding domain of UvrB; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50151; UVR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00204}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00204};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00204};
KW DNA excision {ECO:0000256|ARBA:ARBA00022769, ECO:0000256|HAMAP-
KW Rule:MF_00204};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00204};
KW Excision nuclease {ECO:0000256|ARBA:ARBA00022881, ECO:0000256|HAMAP-
KW Rule:MF_00204};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00204};
KW SOS response {ECO:0000256|ARBA:ARBA00023236, ECO:0000256|HAMAP-
KW Rule:MF_00204}.
FT DOMAIN 26..183
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 431..584
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 632..667
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT COILED 257..284
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 92..115
FT /note="Beta-hairpin"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
SQ SEQUENCE 672 AA; 76714 MW; C4CF3585D08D9EE5 CRC64;
MSKVFKLYSD FQPGGDQPEA IRQLSEGLED GLAHQTLLGV TGSGKTFTIA NVIAKENRPT
MLMAHNKTLA AQLYSEMKAF FPDNAVEYFV SYYDYYQPEA YVPSSDTFIE KDASVNEHIE
QMRLSATKAL LERRDVIVVA SVSAIYGLGD PDSYLKMMLH LTDGMIIDQR AILRRLADLQ
YTRNDQAFTR GTFRVRGEVI DIFPAESDEY ALRVELFDEE VERLSLFDPL TGQIQHRVPR
FTVYPKTHYV TPRERILEAM EQIKVELADR RKVLLENNKL LEEQRITQRT QFDLEMMNEL
GYCSGIENYS RYLSGRAPGE PPPTLFDYLP ADGLLVVDES HVTIPQIGAM YKGDRSRKET
LVEYGFRLPS ALDNRPLRFE EFEALAPQTI YVSATPGNYE IEKSGSEVIE QVVRPTGLLD
PVIEVRPVAT QVDDLLSEIR IRSQKNERVL VTTLTKRMAE DLTEYLEEHG ERVRYLHSDI
DTVERVEIIR DLRLGEFDVL VGINLLREGL DMPEVSLVAI LDADKEGFLR SERSLIQTIG
RAARNLNGKA ILYGDRITNS MEKAIKETER RRAKQIAFNE QHGIVPQGLN KKIGDILQIG
HKVGGKSKGR NKESAKIDKR EDIQLLSTKE LEQRISQLEA QMYKHAQDLE FEAAANVRDQ
LQELRERFIA NS
//
