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Database: UniProt
Entry: I2BE87_SHIBC
LinkDB: I2BE87_SHIBC
Original site: I2BE87_SHIBC 
ID   I2BE87_SHIBC            Unreviewed;       673 AA.
AC   I2BE87; K6UVU3;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=ATP-dependent DNA helicase Rep {ECO:0000256|HAMAP-Rule:MF_01920};
DE            EC=5.6.2.4 {ECO:0000256|HAMAP-Rule:MF_01920};
DE   AltName: Full=DNA 3'-5' helicase Rep {ECO:0000256|HAMAP-Rule:MF_01920};
GN   Name=rep {ECO:0000256|HAMAP-Rule:MF_01920,
GN   ECO:0000313|EMBL:AFJ48841.1};
GN   OrderedLocusNames=EBL_c38060 {ECO:0000313|EMBL:AFJ48841.1};
OS   Shimwellia blattae (strain ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 /
OS   CDC 9005-74) (Escherichia blattae).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shimwellia.
OX   NCBI_TaxID=630626 {ECO:0000313|EMBL:AFJ48841.1, ECO:0000313|Proteomes:UP000001955};
RN   [1] {ECO:0000313|EMBL:AFJ48841.1, ECO:0000313|Proteomes:UP000001955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 / CDC 9005-74
RC   {ECO:0000313|Proteomes:UP000001955};
RX   PubMed=22843577; DOI=10.1128/JB.00829-12;
RA   Brzuszkiewicz E., Waschkowitz T., Wiezer A., Daniel R.;
RT   "Complete genome sequence of the B12-producing Shimwellia blattae strain
RT   DSM 4481, isolated from a cockroach.";
RL   J. Bacteriol. 194:4436-4436(2012).
CC   -!- FUNCTION: Rep helicase is a single-stranded DNA-dependent ATPase
CC       involved in DNA replication; it can initiate unwinding at a nick in the
CC       DNA. It binds to the single-stranded DNA and acts in a progressive
CC       fashion along the DNA in the 3' to 5' direction. {ECO:0000256|HAMAP-
CC       Rule:MF_01920}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034618, ECO:0000256|HAMAP-
CC         Rule:MF_01920};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC         translocating in the 3'-5' direction.; EC=5.6.2.4;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01920};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01920}.
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|ARBA:ARBA00009922, ECO:0000256|HAMAP-Rule:MF_01920}.
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DR   EMBL; CP001560; AFJ48841.1; -; Genomic_DNA.
DR   RefSeq; WP_002444143.1; NZ_BAHA01000027.1.
DR   AlphaFoldDB; I2BE87; -.
DR   STRING; 630626.EBL_c38060; -.
DR   KEGG; ebt:EBL_c38060; -.
DR   PATRIC; fig|630626.3.peg.3710; -.
DR   eggNOG; COG0210; Bacteria.
DR   HOGENOM; CLU_004585_5_2_6; -.
DR   OMA; HCANILI; -.
DR   OrthoDB; 9806690at2; -.
DR   Proteomes; UP000001955; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd17932; DEXQc_UvrD; 1.
DR   CDD; cd18807; SF1_C_UvrD; 1.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   HAMAP; MF_01920; Helicase_Rep; 1.
DR   InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR005752; Helicase_Rep.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   NCBIfam; TIGR01074; rep; 1.
DR   PANTHER; PTHR11070:SF64; ATP-DEPENDENT DNA HELICASE REP; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01920};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_01920}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_01920};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01920, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01920, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Isomerase {ECO:0000256|HAMAP-Rule:MF_01920};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01920}; Reference proteome {ECO:0000313|Proteomes:UP000001955}.
FT   DOMAIN          1..280
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          281..562
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         22..29
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
FT   BINDING         278
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01920"
SQ   SEQUENCE   673 AA;  77226 MW;  4EDB9FAE9FB09E75 CRC64;
     MRLNPGQQQA VDFVTGPCLV LAGAGSGKTR VITNKIAHLI RGCGYQARHI AAVTFTNKAA
     REMKERVAQT LGRKEARGLM ISTFHTLGLE IIKREYAALG MKSNFSLFDD TDQLALIKDL
     TEGLLENDKV IYQQLISTIS NWKNDLMGPD QAAAMARGER DRIFAHCYRL YYDHLKACNV
     LDFDDLILLP TLLLQRNEEV RERWQNKIRY LLVDEYQDTN TSQYELVKLL VGSRARFTVV
     GDDDQSIYSW RGARPQNLVL LSQDFPALQV IKLEQNYRSS GRILKAANIL IANNPHVFEK
     KLFSELGYGP ELKVLSANNE DHEAERVTGE LIAHHFINKT QYKDYAILYR GNHQSRVFEK
     MLMQNRIPYR ISGGTSFFSR PEIKDLLAYL RVLTNPDDDS AFLRIVNTPR REIGPATLQK
     LGEWALQRNK SMFTASFDLG LSQTLTGRGY EALTRFTHWL GEVARLSEKE PVAAVRDLIH
     GIDYESWLFE TSPSPKAAEM RMKNVNQLFT WMTEMLEGSD LEEPMTLTQV VTRFTLRDMM
     ERGESEEELD QVQLMTLHAS KGLEFPYVYL VGMEEGLLPH QSSIDEDNID EERRLAYVGI
     TRAQKELTFT LCKERRQYGE SVRPEPSRFL LELPQDDLQW EVERKKVSAE ERMQKGQAHL
     ASIREQLAKA RKG
//
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