ID   ZORD_ECO24              Reviewed;        1080 AA.
AC   A7ZI07;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Zorya protein ZorD {ECO:0000303|PubMed:29371424};
DE   AltName: Full=Probable ATPase ZorD {ECO:0000303|PubMed:29371424};
GN   Name=zorD {ECO:0000303|PubMed:29371424};
GN   OrderedLocusNames=EcE24377A_0282 {ECO:0000312|EMBL:ABV17208.1};
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1] {ECO:0000312|EMBL:ABV17208.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/JB.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 730-ASP-GLU-731.
RC   STRAIN=E24377A / ETEC;
RX   PubMed=29371424; DOI=10.1126/science.aar4120;
RA   Doron S., Melamed S., Ofir G., Leavitt A., Lopatina A., Keren M.,
RA   Amitai G., Sorek R.;
RT   "Systematic discovery of antiphage defense systems in the microbial
RT   pangenome.";
RL   Science 359:0-0(2018).
CC   -!- FUNCTION: Component of antiviral defense system Zorya type I, composed
CC       of ZorA, ZorB, ZorC and ZorD. Expression of Zorya type I in E.coli
CC       (strain MG1655) confers 10,000-fold resistance to phage SECphi27, 100-
CC       fold resistance to lambda, and 10-fold resistance to T7. While most T7
CC       infected Zorya-containing cells undergo abortive infection, a minority
CC       produce viable phage progeny. These eventually accumulate to a high
CC       multiplicity of infection, leading to culture collapse by 2 hours after
CC       initial infection (PubMed:29371424). ZorA and ZorB probably assemble in
CC       the cell inner membrane and exert their effect there. This may have
CC       ATPase activity (Probable). {ECO:0000269|PubMed:29371424,
CC       ECO:0000305|PubMed:29371424}.
CC   -!- DISRUPTION PHENOTYPE: When this gene is missing the Zorya system does
CC       not confer resistance to SECphi27 in E.coli.
CC       {ECO:0000269|PubMed:29371424}.
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DR   EMBL; CP000800; ABV17208.1; -; Genomic_DNA.
DR   RefSeq; WP_000919796.1; NC_009801.1.
DR   SMR; A7ZI07; -.
DR   EnsemblBacteria; ABV17208; ABV17208; EcE24377A_0282.
DR   KEGG; ecw:EcE24377A_0282; -.
DR   HOGENOM; CLU_000315_21_6_6; -.
DR   OMA; HYTRTWN; -.
DR   Proteomes; UP000001122; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 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.
FT   CHAIN           1..1080
FT                   /note="Zorya protein ZorD"
FT                   /id="PRO_0000456344"
FT   DOMAIN          596..779
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          904..1069
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MUTAGEN         730..731
FT                   /note="DE->AA: No longer resistant to SECphi27."
FT                   /evidence="ECO:0000269|PubMed:29371424"
SQ   SEQUENCE   1080 AA;  122363 MW;  01ABC7C4F3F12D93 CRC64;
     MLKRLLSKLT GNRQQIEHHL KNQYQVEENG LSFPLSLVDD SQLWALASWL EQLAEEDYLI
     SLTDRWLLSW DALYRLLEDE EHASSLPLIG VPDVLPLRAS LSSRGALSDS DFRVWIAEWA
     TLPARKPIRF SRTGAILTHE NQQYLLSREN WALLQATEQL SAQKNQTPGE TTNQLGWAAI
     RKCAKQAAAK FDDYLEKTHV VKPTSLSLRL RKATVADTAV IEIEPHFEDQ PANWLGSFDK
     NSQVHDSYRI PGENGELSHV IIPPEVKEVL NSIHSIPSRR VAGSEALSFV RNPYTFLGED
     AASVIAPEEH EQALFDARIF FHHFRLIPQL NAENKIAEVT LVLEPVSPVP QPEITFGFSA
     PRELDKFIQQ LGISVAAQMP AGSWQGYELE LSQFTEQQWH DCQALLTRWQ QEIEGKEFSD
     VLDIAKYGDR VIGIGEFEKI SSPWLTKAQS ENWLPDDIDF SAFSVETLSG WQPENLHHFD
     ELQERITQAE AVGETHITAP WNDSQLPLDA AKTFSKNWEK QQSTANESQG NVADKTARAV
     LKIEQNIEET AYIKQRRNSL LNARHAEPEI PLSLKEHIRL KDHQREGVAW LQQLFLRSPE
     ETAGCLLADD MGLGKTLQIL SFLVWFIEKF PQEPPSLIVA PVSLLDNWER ELDNFFYTAG
     IPVLKLYGET IKAVKYPKQA IPAHLQSQGI KNLLKPGWQG EAKIILTTYE TLRDQEFSLA
     RQPWSIMVCD EAQKIKNPAA LITHAANAVQ ARFKVACTGT PVENTLVDLW SLFDFAQPGL
     LGALNEFGKH YVRPIENEDG RDTERLESLR ALIEPQTLRR TKEEVARDLP QKIEVESCKQ
     LTLSGVQKQL YLSSVANWQQ QQALSEGMQQ AGTGMLGLLH RLKLICAHPA VVNPEPRFRD
     NSPKLNWLLK ILAELKHTTK DKVIIFTELR DLQRELQHAI HQKFGFRPVI INGDTSTKSQ
     SQNSRQRLID DFQAQPGFGV IILSTVAVGF GVNVQKANHV IHFTRCWNPA KEDQATDRAY
     RIGQTKDVYV YYPTVKDTEI TTFEETLDDL LQRRRALARD MLCATPDLSG ADFEAILKGA