ID   GLND_BORA1              Reviewed;         858 AA.
AC   Q2L165;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=[Protein-PII] uridylyltransferase;
DE            Short=PII uridylyl-transferase;
DE            EC=2.7.7.59;
DE   AltName: Full=Uridylyl-removing enzyme;
DE   AltName: Full=UTase;
GN   Name=glnD; OrderedLocusNames=BAV1732;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
CC   -!- FUNCTION: Modifies, by uridylylation or deuridylylation the PII
CC       (glnB) regulatory protein (By similarity).
CC   -!- CATALYTIC ACTIVITY: UTP + [protein-PII] = diphosphate + uridylyl-
CC       [protein-PII].
CC   -!- SIMILARITY: Belongs to the glnD family.
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DR   EMBL; AM167904; CAJ49340.1; -; Genomic_DNA.
DR   RefSeq; YP_786250.1; -.
DR   GeneID; 6266904; -.
DR   GenomeReviews; AM167904_GR; BAV1732.
DR   KEGG; bav:BAV1732; -.
DR   NMPDR; fig|521.1.peg.1689; -.
DR   HOGENOM; Q2L165; -.
DR   OMA; Q2L165; MQHDLFH.
DR   GO; GO:0008773; F:[protein-PII] uridylyltransferase activity; IEA:HAMAP.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   HAMAP; MF_00277; -; 1.
DR   InterPro; IPR002912; ACT_bd.
DR   InterPro; IPR010043; GlnD_Uridyltrans.
DR   InterPro; IPR003607; Met-dep_phosphohydro_HD.
DR   InterPro; IPR006674; Met-dep_phosphohydro_HD_sub.
DR   InterPro; IPR002934; Nucleotidyltransferase.
DR   InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
DR   PANTHER; PTHR13734:SF1; GlnD_Uridyltrans; 1.
DR   Pfam; PF01842; ACT; 2.
DR   Pfam; PF08335; GlnD_UR_UTase; 1.
DR   Pfam; PF01966; HD; 1.
DR   Pfam; PF01909; NTP_transf_2; 1.
DR   PIRSF; PIRSF006288; PII_uridyltransf; 1.
DR   SMART; SM00471; HDc; 1.
DR   TIGRFAMs; TIGR01693; UTase_glnD; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Nucleotidyltransferase; Transferase.
FT   CHAIN         1    858       [Protein-PII] uridylyltransferase.
FT                                /FTId=PRO_1000022326.
SQ   SEQUENCE   858 AA;  97978 MW;  DE261EA92F0D5AB7 CRC64;
     MNPTDLHPIK ERMQAARAAA IADFRQHLRP DPLLSELRRI VDQALRDLLK LCPLPAGATL
     AAVGGYGRGE LYPHSDVDLL ILLPRAPDGP DESAIETLVA SLWDLGLEPG HSVRTLAECE
     TEASADITVE TALLESRWLA GSRSLMKQFE TAMTARLDAR AFFRAKRVEM QQRHARYQDT
     PYALEPNSKE SPGGLRDLQV ILWMARAAGF GRNWRAVAQA GLLTAPEARD LRRAEQAFKR
     LRIELHLLTR RREDRLLFDL QPTLAEVYGI ATTTTRRASE LLMQRYYWAA RLVTQLNVIL
     IQNIEERLFP RPESDARAID EEFRSLHGRL DIIREDCFER NPTLLLRAFL VMQQHPGLSG
     MSARTLRAIW HSRHRIDAQF RRNPVNRKLF LQILQQPRGI VHELRRMTML NILPRYLPVF
     RRIVGQMQHD LFHVYTVDQH TLAVIRNLRR FTMPEHASEY PLASQVMAGL DRHWLLYVAA
     LFHDIAKGRG GDHSELGARD ARRFAQEHGL APEDAELVEF LVRQHLLMSA VAQKRDLSDP
     EVINEFARQV KDERHLNALY LLTVADIRGT SPKVWNAWKG KLLEDLYRLT LAALGGAQDT
     RTVLAERKEE AARLLRLAGL RDDARDAFWQ QLDVAYFLRH DASEIAWHTR HLYYQVQPDK
     PVVKVRPTEE GSGLQIMVYT RDTPDLFMNT CAYFDGKAFS IQDARIHTTR QGWALDSFIV
     LPAEPLADLR AQAALVEHEL AERLRQAQGG ARLADVRVFH RNRQSRVSRV FPVMPQAELH
     PDERSQSWRL SVTATDRPGL LHALARVMAE NGVNLIMAKI MTLGDRVEDV FIISGAVLER
     PRTQMQFEHA VLDALAGE
//