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Database: UniProt
Entry: A0A090TBK7_9VIBR
LinkDB: A0A090TBK7_9VIBR
Original site: A0A090TBK7_9VIBR 
ID   A0A090TBK7_9VIBR        Unreviewed;       676 AA.
AC   A0A090TBK7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
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   ORFNames=JCM19240_3202 {ECO:0000313|EMBL:GAL37340.1};
OS   Vibrio maritimus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=990268 {ECO:0000313|EMBL:GAL37340.1, ECO:0000313|Proteomes:UP000029224};
RN   [1] {ECO:0000313|EMBL:GAL37340.1, ECO:0000313|Proteomes:UP000029224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 19240 {ECO:0000313|EMBL:GAL37340.1,
RC   ECO:0000313|Proteomes:UP000029224};
RA   Sawabe T., Meirelles P., Nakanishi M., Sayaka M., Hattori M., Ohkuma M.;
RT   "Vibrio maritimus JCM 19240. (C210) whole genome shotgun sequence.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAL37340.1, ECO:0000313|Proteomes:UP000029224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 19240 {ECO:0000313|EMBL:GAL37340.1,
RC   ECO:0000313|Proteomes:UP000029224};
RG   NBRP consortium;
RA   Sawabe T., Meirelles P., Nakanishi M., Sayaka M., Hattori M., Ohkuma M.;
RL   Submitted (SEP-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAL37340.1}.
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DR   EMBL; BBMT01000016; GAL37340.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A090TBK7; -.
DR   OrthoDB; 9806651at2; -.
DR   Proteomes; UP000029224; Unassembled WGS sequence.
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}; 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:UP000029224};
KW   SOS response {ECO:0000256|ARBA:ARBA00023236, ECO:0000256|HAMAP-
KW   Rule:MF_00204}.
FT   DOMAIN          26..159
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          432..594
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          636..671
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
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   676 AA;  76286 MW;  BB0211134344E11E CRC64;
     MAKHFELVSD YKPSGDQPTA IAQLVDGLDS GLAHQTLLGV TGSGKTFTLA NVIAQAQRPA
     ILLAPNKTLA AQLYGEMKAF FPNNAVEYFV SYYDYYQPEA YVPTTDTFIE KDASVNAHIE
     QMRLSATKAL LERKDAIIVA SVSAIYGLGD PDSYLKMMLH VTRGAVIDQR DILLRLAELQ
     YSRNDVAFER GQFRVRGEVI DIFPAESDQE AVRLEMFDDE IDCISLFDPL TGVITQRDIA
     RYTIYPKTHY VTPRERILDA IEEIKKELTS RATYLKENNK LLEEQRISQR TQFDIEMMNE
     LGFCSGIENY SRYLSGRKEG EPPPTLFDYL PADGLLIIDE SHVTVPQIGA MYKGDRSRKE
     TLVEFGFRLP SALDNRPMKF EEFEMISPQT IFVSATPSAY ELEKSNGDVA DQVVRPTGLL
     DPEIEVRPVA TQVDDLLSEA KARAAIEERV LVTTLTKRMA EDLTEYLNEH GVKVRYLHSD
     IDTVERTEII RDLRLGEFDV LVGINLLREG LDMPEVSLVA ILDADKEGFL RSERSLIQTI
     GRAARNIKGK AILYGDRITK SMQKAIDETS RRREKQHAYN EKMGLVPTAL KRNIKDIMEI
     GGVVKGGKPK KGKQVPLSKV AEPSQAYVAL SSQDLEKQIL KLEGEMYQHA QNLEFELAAE
     KRDEIEKLRQ HFIANS
//
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