ID   ABPB_ECOLI              Reviewed;         729 AA.
AC   P52126; Q2MAE4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Anti-bacteriophage protein B {ECO:0000303|PubMed:25224971};
DE   AltName: Full=Probable helicase AbpB {ECO:0000305};
GN   Name=abpB {ECO:0000303|PubMed:25224971}; Synonyms=yfjK;
GN   OrderedLocusNames=b2627, JW2608;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [3]
RP   FUNCTION IN ANTIVIRAL DEFENSE, INTERACTION WITH ABPA, SUBUNIT, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=K12 /MH1;
RX   PubMed=25224971; DOI=10.1266/ggs.89.51;
RA   Yasui R., Washizaki A., Furihata Y., Yonesaki T., Otsuka Y.;
RT   "AbpA and AbpB provide anti-phage activity in Escherichia coli.";
RL   Genes Genet. Syst. 89:51-60(2014).
RN   [4]
RP   FUNCTION IN RADIATION RESISTANCE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   ALA-152.
RC   STRAIN=K12;
RX   PubMed=24596148; DOI=10.7554/elife.01322;
RA   Byrne R.T., Klingele A.J., Cabot E.L., Schackwitz W.S., Martin J.A.,
RA   Martin J., Wang Z., Wood E.A., Pennacchio C., Pennacchio L.A., Perna N.T.,
RA   Battista J.R., Cox M.M.;
RT   "Evolution of extreme resistance to ionizing radiation via genetic
RT   adaptation of DNA repair.";
RL   Elife 3:e01322-e01322(2014).
CC   -!- FUNCTION: Part of an antiviral system composed of AbpA and AbpB; when
CC       both are expressed from a plasmid they confer resistance to phages T2,
CC       T4, T7 and lambda but not RB32 or RB69. Resistance is temperature
CC       dependent, it can be seen at 30 degrees Celsius but not at 37 or 42
CC       degrees Celsius. The system impairs phage but not bacterial DNA
CC       synthesis (shown for T4, T7 and lambda). Partially suppressed by
CC       mutations in T4 gene 41, a replicative helicase.
CC       {ECO:0000269|PubMed:25224971}.
CC   -!- FUNCTION: Deletion or mutations in this gene were selected in directed
CC       evolution experiments for resistance to intense ionizing radiation
CC       (3000 Gy). {ECO:0000269|PubMed:24596148}.
CC   -!- SUBUNIT: Interacts with AbpB. {ECO:0000269|PubMed:25224971}.
CC   -!- DISRUPTION PHENOTYPE: About 20% increase in T4 progeny; the phenotype
CC       is the same in a double abpA-abpB deletion (PubMed:25224971). 10-fold
CC       increased survival following 3000 Gy ionizing radiation
CC       (PubMed:24596148). {ECO:0000269|PubMed:24596148,
CC       ECO:0000269|PubMed:25224971}.
CC   -!- MISCELLANEOUS: Part of prophage CP4-57. {ECO:0000269|PubMed:9278503}.
CC   -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
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DR   EMBL; U36840; AAA79796.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75675.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76762.1; -; Genomic_DNA.
DR   PIR; T08639; T08639.
DR   RefSeq; NP_417116.1; NC_000913.3.
DR   RefSeq; WP_000136402.1; NZ_LN832404.1.
DR   AlphaFoldDB; P52126; -.
DR   SMR; P52126; -.
DR   BioGRID; 4260623; 76.
DR   BioGRID; 851446; 3.
DR   DIP; DIP-12076N; -.
DR   IntAct; P52126; 23.
DR   STRING; 511145.b2627; -.
DR   PaxDb; 511145-b2627; -.
DR   EnsemblBacteria; AAC75675; AAC75675; b2627.
DR   GeneID; 947111; -.
DR   KEGG; ecj:JW2608; -.
DR   KEGG; eco:b2627; -.
DR   PATRIC; fig|511145.12.peg.2722; -.
DR   EchoBASE; EB2989; -.
DR   eggNOG; COG1204; Bacteria.
DR   HOGENOM; CLU_025497_0_0_6; -.
DR   InParanoid; P52126; -.
DR   OMA; GAQFYML; -.
DR   OrthoDB; 9815222at2; -.
DR   BioCyc; EcoCyc:G7362-MONOMER; -.
DR   PRO; PR:P52126; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0051607; P:defense response to virus; IMP:EcoCyc.
DR   GO; GO:0010212; P:response to ionizing radiation; IMP:EcoCyc.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR   PANTHER; PTHR12131:SF1; ATP-DEPENDENT RNA HELICASE SUPV3L1, MITOCHONDRIAL; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 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.
PE   1: Evidence at protein level;
KW   Antiviral defense; ATP-binding; Helicase; Hydrolase; Nucleotide-binding;
KW   Reference proteome; Stress response.
FT   CHAIN           1..729
FT                   /note="Anti-bacteriophage protein B"
FT                   /id="PRO_0000169276"
FT   DOMAIN          109..271
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          297..472
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   BINDING         122..129
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MUTAGEN         152
FT                   /note="A->D: 100-fold increased survival following 3000 Gy
FT                   ionizing radiation."
FT                   /evidence="ECO:0000269|PubMed:24596148"
SQ   SEQUENCE   729 AA;  83062 MW;  CB65BCD1B36FBFAF CRC64;
     MTEIYEQAKH SLQGEDFSSF NYLFAVNKLL SNPVSYDLGR DLIVRALDSR ERFSEHTTIL
     KNMVRKSGLF PYLKKEFTSL TPDDLRVLEL YRTPFSDGYV FHSMQFHIFD LLKSGQNVVL
     SAPTSMGKSA IVDSLLGMGT LKRLVLVVPT VALADETRRR LQERFGDRYQ IIHHSSQVCH
     SDQAVYVLTQ ERVNERDDIV DIDLFVIDEF YKLAFRQLKS GDIDHQDERV IELNIALSKL
     LKVSRQFYLT GPFVNSIRGL EKLGYPHTFV STDFNTVALD VKTFGIKAND DKAKLKALGE
     IAHACVDATI IYCKSPTVAG LVARELIRLG HGTPTENPHV DWVSEEFDAD WDYTVALRNG
     IGLHFGALPR ALQQYTADQF NAGKLRFLLC TSTIIEGVNT IAKNVVIYDN RDGTRSIDKF
     THGNIKGRAG RMGVHFVGKI FCLEEIPEDN LNQEVDIPLG IQGIDTPINL LASVQPDHLS
     EFSQDRFDEV FINDRVSIDL VKKHSYFRVE QFEMLQSMFE MMDDNEFSSL VFHWTPATNF
     LKTFAKIIAR LVPHTFSRNG VPVKPTDVMI AKLAGYLSAE SYSEYLKNQI DYARQWISEG
     EKRTLSIALN NDLKLITNTF GYTLPKVLSL MEDVVKHHAV KRGIRSKVDY THVKLAFESF
     HLPPGVNALE EIGIPIQTLH RLVDLLEFSD EADVDELSQY LRDTQDIWSR SIGYVDQMFI
     RRALGIRRH
//