ID   REP_BPCHP               Reviewed;         399 AA.
AC   P19189; P19186;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Replication-associated protein ORF4;
DE            EC=3.1.21.-;
DE            EC=6.5.1.1;
DE   AltName: Full=Rep;
GN   ORFNames=ORF4;
OS   Chlamydia phage 1 (Bacteriophage Chp1).
OC   Viruses; Monodnaviria; Sangervirae; Phixviricota; Malgrandaviricetes;
OC   Petitvirales; Microviridae; Gokushovirinae; Chlamydiamicrovirus.
OX   NCBI_TaxID=2003327;
OH   NCBI_TaxID=83554; Chlamydia psittaci (Chlamydophila psittaci).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2607341; DOI=10.1099/0022-1317-70-12-3381;
RA   Storey C.C., Lusher M., Richmond S.J.;
RT   "Analysis of the complete nucleotide sequence of Chp1, a phage which
RT   infects avian Chlamydia psittaci.";
RL   J. Gen. Virol. 70:3381-3390(1989).
CC   -!- FUNCTION: Plays an essential role in viral DNA replication. Binds the
CC       origin of replication and cleaves the dsDNA replicative form I (RFI)
CC       and becomes covalently bound to it via phosphotyrosine bond, generating
CC       the dsDNA replicative form II (RFII). In turn, viral DNA replication
CC       initiates at the 3'-OH of the cleavage site. After one round of rolling
CC       circle synthesis, protein ORF4 is linked to the newly synthesized ssDNA
CC       and joins the ends of the displaced strand to generate a circular
CC       single-stranded molecule ready to be packed into a virion.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC         diphosphate.; EC=6.5.1.1;
CC   -!- SIMILARITY: Belongs to the microviridae Rep protein family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA00512.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; D00624; BAA00511.1; -; Genomic_DNA.
DR   EMBL; D00624; BAA00512.1; ALT_INIT; Genomic_DNA.
DR   Proteomes; UP000002125; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   ATP-binding; Endonuclease; Hydrolase; Ligase; Nuclease; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..399
FT                   /note="Replication-associated protein ORF4"
FT                   /id="PRO_0000066092"
FT   ACT_SITE        251
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        255
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   399 AA;  47560 MW;  B27A7834D29D1990 CRC64;
     MRYSLDSYLI SVYIRLTQRK SDYMCTNPII PIVQYKVPVK SSLDVVDWSK FRSNFKANLF
     FFEKNVVRRA VSNVDEAFRF TEQLKQVSYL STFDLDGYHQ VKQFSFPLPC RKCSECLQKR
     SKDLAVQATM EARSHEENSV LILTYDNDHL GDNILDYDHI RVFQKRLRRY VDYHYGKKIK
     FLTVGEYGDK KGRMHWHMIV FGWKPKSEEQ LEPYLGGKYR TDVRYRSRKL KELWKFGYVD
     VDEATDGNIF YVARYVQKKF VVGCDLDSSK SSSRREKKTA SQALGLDYFF SYLRQFLKTK
     RIVLNGFRYG FPRYFKDLLR KLVSEDSEFD TEYYNALRKR LLSVCSYSMV NKYFTYLECL
     VEVLPVLNFH DLYQRALRYM DQSILKPHAS DHDGEYNTT