GLNB_MYCTU
ID GLNB_MYCTU Reviewed; 112 AA.
AC P9WN31; L0TB95; P64249; Q10960;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Nitrogen regulatory protein P-II;
GN Name=glnB; OrderedLocusNames=Rv2919c; ORFNames=MTCY338.08c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: In nitrogen-limiting conditions, when the ratio of Gln to 2-
CC ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP
CC allows the deadenylation of glutamine synthetase (GS), thus activating
CC the enzyme. Conversely, in nitrogen excess P-II is deuridylated and
CC promotes the adenylation of GS. P-II indirectly controls the
CC transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed
CC conversion of NR-I to NR-I-phosphate, the transcriptional activator of
CC glnA. When P-II is uridylylated to P-II-UMP, these events are reversed
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the P(II) protein family. {ECO:0000255|PROSITE-
CC ProRule:PRU00675}.
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DR EMBL; AL123456; CCP45721.1; -; Genomic_DNA.
DR PIR; G70747; G70747.
DR RefSeq; NP_217435.1; NC_000962.3.
DR RefSeq; WP_003414756.1; NZ_NVQJ01000006.1.
DR PDB; 3BZQ; X-ray; 1.40 A; A=1-112.
DR PDB; 3LF0; X-ray; 2.40 A; A/B/C=1-112.
DR PDBsum; 3BZQ; -.
DR PDBsum; 3LF0; -.
DR AlphaFoldDB; P9WN31; -.
DR SMR; P9WN31; -.
DR STRING; 83332.Rv2919c; -.
DR PaxDb; P9WN31; -.
DR DNASU; 887756; -.
DR GeneID; 45426906; -.
DR GeneID; 887756; -.
DR KEGG; mtu:Rv2919c; -.
DR TubercuList; Rv2919c; -.
DR eggNOG; COG0347; Bacteria.
DR OMA; HQIEVNF; -.
DR PhylomeDB; P9WN31; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0043531; F:ADP binding; IDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IDA:MTBBASE.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0051701; P:biological process involved in interaction with host; IMP:MTBBASE.
DR GO; GO:0006808; P:regulation of nitrogen utilization; IBA:GO_Central.
DR Gene3D; 3.30.70.120; -; 1.
DR InterPro; IPR002187; N-reg_PII.
DR InterPro; IPR011322; N-reg_PII-like_a/b.
DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR InterPro; IPR017918; N-reg_PII_CS.
DR InterPro; IPR002332; N-reg_PII_urydylation_site.
DR PANTHER; PTHR30115; PTHR30115; 1.
DR Pfam; PF00543; P-II; 1.
DR PIRSF; PIRSF039144; GlnB; 1.
DR PRINTS; PR00340; PIIGLNB.
DR SMART; SM00938; P-II; 1.
DR SUPFAM; SSF54913; SSF54913; 1.
DR PROSITE; PS00638; PII_GLNB_CTER; 1.
DR PROSITE; PS51343; PII_GLNB_DOM; 1.
DR PROSITE; PS00496; PII_GLNB_UMP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..112
FT /note="Nitrogen regulatory protein P-II"
FT /id="PRO_0000139779"
FT MOD_RES 51
FT /note="O-UMP-tyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00675"
FT STRAND 1..8
FT /evidence="ECO:0007829|PDB:3BZQ"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:3BZQ"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:3BZQ"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:3BZQ"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:3LF0"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:3LF0"
FT STRAND 55..66
FT /evidence="ECO:0007829|PDB:3BZQ"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:3BZQ"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:3BZQ"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:3BZQ"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:3LF0"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:3BZQ"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:3BZQ"
SQ SEQUENCE 112 AA; 12227 MW; 1AE59B5537CB3894 CRC64;
MKLITAIVKP FTLDDVKTSL EDAGVLGMTV SEIQGYGRQK GHTEVYRGAE YSVDFVPKVR
IEVVVDDSIV DKVVDSIVRA ARTGKIGDGK VWVSPVDTIV RVRTGERGHD AL
