ID D8MK72_ERWBE Unreviewed; 1855 AA.
AC D8MK72;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Conjugal transfer nickase/helicase {ECO:0000313|EMBL:CAX53670.1};
GN Name=traI {ECO:0000313|EMBL:CAX53670.1};
GN OrderedLocusNames=EbC_pEb17202170 {ECO:0000313|EMBL:CAX53670.1};
OS Erwinia billingiae (strain Eb661).
OG Plasmid pEB170 {ECO:0000313|EMBL:CAX53670.1,
OG ECO:0000313|Proteomes:UP000008793}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=634500 {ECO:0000313|Proteomes:UP000008793};
RN [1] {ECO:0000313|EMBL:CAX53670.1, ECO:0000313|Proteomes:UP000008793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eb661 {ECO:0000313|EMBL:CAX53670.1,
RC ECO:0000313|Proteomes:UP000008793};
RC PLASMID=pEB170 {ECO:0000313|EMBL:CAX53670.1};
RX PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA Knaust F., Geider K., Reinhardt R.;
RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT tasmaniensis with the pear pathogen E. pyrifoliae.";
RL BMC Genomics 11:393-393(2010).
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DR EMBL; FP236830; CAX53670.1; -; Genomic_DNA.
DR RefSeq; WP_013200037.1; NC_014305.1.
DR KEGG; ebi:EbC_pEb17202170; -.
DR HOGENOM; CLU_001748_2_1_6; -.
DR Proteomes; UP000008793; Plasmid pEB170.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR009767; DNA_helicase_TraI_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014059; TraI/TrwC_relax.
DR InterPro; IPR040668; TraI_2B.
DR InterPro; IPR040987; TraI_N.
DR InterPro; IPR014862; TrwC.
DR NCBIfam; NF041492; MobF; 1.
DR NCBIfam; TIGR02686; relax_trwC; 1.
DR Pfam; PF13604; AAA_30; 1.
DR Pfam; PF18272; ssDNA_TraI_N; 1.
DR Pfam; PF18340; TraI_2B; 1.
DR Pfam; PF07057; TraI_C; 1.
DR Pfam; PF08751; TrwC; 1.
DR SUPFAM; SSF55464; Origin of replication-binding domain, RBD-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:CAX53670.1};
KW Helicase {ECO:0000313|EMBL:CAX53670.1};
KW Hydrolase {ECO:0000313|EMBL:CAX53670.1};
KW Nucleotide-binding {ECO:0000313|EMBL:CAX53670.1};
KW Plasmid {ECO:0000313|EMBL:CAX53670.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008793}.
FT DOMAIN 10..273
FT /note="TrwC relaxase"
FT /evidence="ECO:0000259|Pfam:PF08751"
FT DOMAIN 628..680
FT /note="TraI N-terminal subdomain"
FT /evidence="ECO:0000259|Pfam:PF18272"
FT DOMAIN 686..764
FT /note="TraI 2B/2B-like"
FT /evidence="ECO:0000259|Pfam:PF18340"
FT DOMAIN 1480..1632
FT /note="DNA helicase TraI type C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07057"
FT REGION 266..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1793..1855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1834..1855
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1855 AA; 200990 MW; 49D38ED589B794C2 CRC64;
MMTVAPVASA ADAAGYYSSK DNYYFLDDLQ SQWLGEGARE LGLEGPVDLD AFTAVLHGKL
PNGVELGKEV QGNHVHRPGH DFTFSAPKSI SMLILAGGDR RLLEAHHEAV KETLAVMEQM
VSARDTKDGI TSIVPTGKMV AALFTHDTSR NLDPQIHTHA VLANVTELEG KWKALATDYV
HGAGFIETMY RHQVSFGKIY RNALKGKTEA LGFETELTGG KHELWEVKGF SDEVLDVFSS
RYREIHARVG DEASLKSRDV AALDTRQRKQ DISRYGEDTA AMPVTEALTR TRAQPEAGIS
REDGPAGRAE KHPGPAKEMP ISKPETADGR SRLQDRWQRQ MDDLGFDLSG VMKEATLRAA
KRPLPGEERP LPPDAMMAVR TAISVLSDSR TRFTYGDLLM TAHEAGEAQQ SVPHLRQAID
RAVSENLLAP LDGDKGVFTS HIHLLDELSV QALAADIVKE NKVVSFRSPE NEAPARLRGV
EFAPVAILSA PASVQRLRET TEELVTMSRE NGREVKVLAS SAERGMSLGK SALLKDDILY
RSRVLDSTFS LSPQSTLIVE GAEKLGLKEM LVLTGEAREK NAQLLFLDSP GRQSNANALS
VLSSAGVERH GLTEPAPGLE ARVISIGDKR DRYRALAERY ADLSGLDATV TASVVGAREQ
QQLTGLIRDA LQNAGKLGRE DVSIEARTPV FMTAKERRLP ASWQAGMVLE DRSEKSETRH
YVIDRVHAET RMLSLVDGDG VLSRLKLGEL TGDWRAFTAE KISVAQGEQL FALAADKTTG
LKAHDRLTVT AVEKDGLTLM RAGQGKPLRV PTDRPLYVTH GYVSAPGSRD NEQGTVLASL
NARDLSANMM NALAQSGHEA EIFTGEALSR AEERLGRMRT TRSPLALVRQ ASGKEETGEA
LTALNAAVRT DVQKAVSRAV AQMRDVSFSE VKLLDQAVSF TDDVGALRGE IARLAKAGDL
MPVKVGGEPR YVARATWEME KMIIGEITAG KNTQMPLMPE VPPSLLSGLT DGQKGATTLI
LQSTDRFTAV QGYAGVGKTT QFAAVKAAID TLPEGERPLI IGLAPTHRAV KEMRDVGIDA
QTLKSFVMDW QQRSAAGESV RYDKTLFLID ESSMLGNQDT AAAYRAIAAG DGRAVPVGDV
AQLESPESGA PFRLMQERSP IDVAVMKEIV RQRDANLKSA VYSVIENKAG AALEKIEQVS
PLTVPRRAGA VPPSRSVVET QDPVAFIVAD YMSRTDVARE ETMILVQLHA DRRAINSGIH
NAMVATKELG DKAVTVPVLD RVTGGRHDFN RIQDWKTGQM VLANERYLSV TGVDRGTGRV
LLRDENGRMQ YYSPAELNAT EIEVFEKRNI ELREGDSVRL NKTQKRAGHA AHEQYRVEAL
RDNGEIVLRN RDGVKVIDPA AVTADRHVDY AWAVTGYGGQ GASAAYDIVL EGTEGARERM
SGMRAFYINV SRVRDHVQVV TDGLDKWVAT LREKDTGPAT AHDALTPEPA RAQARSIWAM
GQAVSKTAIG RAFLREQGLK DSPVTARVIP PTHKYPVPHL TLPAYDGNGK SAGLTLIPLQ
PDTGRIKAGE VRQLVTNGAQ AAILQKSRSG QTLIVSDLTQ GLAAARDNPA SGVLLLTGRH
APSAQLLKVA GGLPDRATRP DATLLRLVQS ELQAVLRDLP PDAPVPDERT ALRAALEAVE
KAQLAQEIRM PPETLAQQTG TSLPDVTREL ASRIEERMKQ QIPPLPGEKV PDYASLVRDA
SAALAGSDAL PGGAVRAVLS ALSGSGLSAD MRLSGDVTQG GGVPASVLKQ VHEEQARGRT
QAGPEQPAVS GKALAGAVRE LDRQHAPELP PAPRGQEMEH KELNHEPQRH IQKER
//