ID B3PKF7_CELJU Unreviewed; 675 AA.
AC B3PKF7;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 103.
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 ECO:0000313|EMBL:ACE84767.1};
GN OrderedLocusNames=CJA_2425 {ECO:0000313|EMBL:ACE84767.1};
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211 {ECO:0000313|EMBL:ACE84767.1, ECO:0000313|Proteomes:UP000001036};
RN [1] {ECO:0000313|EMBL:ACE84767.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107 {ECO:0000313|EMBL:ACE84767.1};
RX PubMed=18556790; DOI=10.1128/JB.01701-07;
RA Deboy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
RN [2] {ECO:0000313|EMBL:ACE84767.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ueda107 {ECO:0000313|EMBL:ACE84767.1};
RA DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Daugherty S.C.,
RA Khouri H.M., Emerson J.B., Mohamoud Y., Watkins K.L., Henrissat B.,
RA Gilbert H.J., Nelson K.E.;
RL Submitted (JAN-2008) 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; CP000934; ACE84767.1; -; Genomic_DNA.
DR RefSeq; WP_012488023.1; NC_010995.1.
DR AlphaFoldDB; B3PKF7; -.
DR STRING; 498211.CJA_2425; -.
DR KEGG; cja:CJA_2425; -.
DR eggNOG; COG0556; Bacteria.
DR HOGENOM; CLU_009621_2_1_6; -.
DR OrthoDB; 9806651at2; -.
DR Proteomes; UP000001036; 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; 6.10.140.240; -; 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}; Reference proteome {ECO:0000313|Proteomes:UP000001036};
KW SOS response {ECO:0000256|ARBA:ARBA00023236, ECO:0000256|HAMAP-
KW Rule:MF_00204}.
FT DOMAIN 31..164
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 435..601
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 638..673
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT COILED 262..289
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 97..120
FT /note="Beta-hairpin"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
FT BINDING 44..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
SQ SEQUENCE 675 AA; 76822 MW; 36132D1A5370FD00 CRC64;
MTKSFESKQF VVHSEFAPAG DQPSAIAGLV AGIEAGLAHQ TLLGVTGSGK TFTIANVIAR
VQRPTLIMAH NKTLAAQLYG EFKEFFPNNA VEYFVSYYDY YQPEAYVPSS DTFIEKDSSV
NEHIEQMRLS ATKALMERKD AIIVATVSAI YGLGDPDSYM KMLLHIVRGD RIDQRQILRR
LAELQYTRND MDFSRATYRV RGEVIDIYPA DSDMEAVRVE LFDDEVEQIS VFDPLTGEVL
HKVPRYTIYP KTHYVTPRET VLEAIDNIKE ELRERLAYLR ENNKLVEAQR LEQRTRYDLE
MMHELGYCNG IENYSRFLSG RTSGEPPPTL FDYLPADALL VIDESHVTVP QIGAMYKGDR
SRKETLVEYG FRLPSALDNR PMRFDEWERI APQMIFVSAT PGKYEDEHQG QVVEQVVRPT
GLVDPQIEVR PAGTQVDDVL SEIRLRAEKN ERVLVTTLTK RMAEDLTEYL AEHGVRVRYL
HSDIDTVERV EIIRDLRLGQ FDVLVGINLL REGLDMPEVS LVAILDADKE GFLRSDRSLI
QTIGRAARNV NGKAILYADN MTGSMKRAID ETERRRQKQI DHNRKQGITP QGIRKQIADI
LEGAQVPGAG GRSARNKAMA IAEKQGKYKV EVNPKDIWKT IELLEKQMFQ AAKDLEFEVA
AKLRDEIEKL KKQAV
//
