CHIZ_MYCTU
ID CHIZ_MYCTU Reviewed; 165 AA.
AC I6YA32;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Cell wall hydrolase ChiZ {ECO:0000305};
DE EC=3.4.-.- {ECO:0000305|PubMed:16942606};
GN Name=chiZ {ECO:0000303|PubMed:16942606};
GN OrderedLocusNames=Rv2719c {ECO:0000312|EMBL:CCP45517.1};
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 INDUCTION.
RX PubMed=16885473; DOI=10.1128/jb.00340-06;
RA Brooks P.C., Dawson L.F., Rand L., Davis E.O.;
RT "The mycobacterium-specific gene Rv2719c is DNA damage inducible
RT independently of RecA.";
RL J. Bacteriol. 188:6034-6038(2006).
RN [3]
RP FUNCTION, CELL WALL HYDROLASE ACTIVITY, SUBCELLULAR LOCATION, INDUCTION,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=16942606; DOI=10.1111/j.1365-2958.2006.05333.x;
RA Chauhan A., Lofton H., Maloney E., Moore J., Fol M., Madiraju M.V.,
RA Rajagopalan M.;
RT "Interference of Mycobacterium tuberculosis cell division by Rv2719c, a
RT cell wall hydrolase.";
RL Mol. Microbiol. 62:132-147(2006).
RN [4]
RP FUNCTION, INTERACTION WITH FTSI AND FTSQ, AND DISRUPTION PHENOTYPE.
RX PubMed=22094151; DOI=10.1016/j.tube.2011.10.022;
RA Vadrevu I.S., Lofton H., Sarva K., Blasczyk E., Plocinska R.,
RA Chinnaswamy J., Madiraju M., Rajagopalan M.;
RT "ChiZ levels modulate cell division process in mycobacteria.";
RL Tuberculosis 91:S128-S135(2011).
CC -!- FUNCTION: Cell wall hydrolase that modulates cell division process
CC (PubMed:22094151, PubMed:16942606). Probably acts by modulating FtsZ
CC ring assembly (PubMed:16942606, PubMed:22094151). Murein hydrolase
CC activity is targeted to sites of nascent peptidoglycan (PG) synthesis
CC (PubMed:16942606). Overproduction compromises midcell localization of
CC FtsZ rings, but has no effect on the intracellular levels of FtsZ
CC (PubMed:16942606). {ECO:0000269|PubMed:16942606,
CC ECO:0000269|PubMed:22094151}.
CC -!- SUBUNIT: Interacts with the cell division proteins FtsI and FtsQ.
CC {ECO:0000269|PubMed:22094151}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000255}. Note=Localizes at poles and at midcell regions.
CC {ECO:0000269|PubMed:16942606}.
CC -!- INDUCTION: Up-regulated in the presence of nitric oxide, reactive
CC oxygen intermediates, mitomycin C, cephalexin or during growth in
CC macrophages (PubMed:16942606). Expression is strongly DNA damage
CC inducible independently of RecA (PubMed:16885473). Down-regulated under
CC hypoxic growth conditions (PubMed:16942606).
CC {ECO:0000269|PubMed:16885473, ECO:0000269|PubMed:16942606}.
CC -!- DISRUPTION PHENOTYPE: Mutants have stable FtsZ rings (PubMed:22094151).
CC Deletion mutant is more sensitive to DNA damage (PubMed:16942606).
CC Deletion of the gene causes a 10% increase in average cell length
CC (PubMed:16942606). Loss of the gene does not influence the growth of
CC M.tuberculosis in mice lungs and spleen (PubMed:22094151).
CC {ECO:0000269|PubMed:16942606, ECO:0000269|PubMed:22094151}.
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DR EMBL; AL123456; CCP45517.1; -; Genomic_DNA.
DR RefSeq; NP_217235.1; NC_000962.3.
DR RefSeq; WP_003899446.1; NZ_NVQJ01000017.1.
DR AlphaFoldDB; I6YA32; -.
DR SMR; I6YA32; -.
DR STRING; 83332.Rv2719c; -.
DR PaxDb; I6YA32; -.
DR DNASU; 887959; -.
DR GeneID; 887959; -.
DR KEGG; mtu:Rv2719c; -.
DR PATRIC; fig|83332.111.peg.3025; -.
DR TubercuList; Rv2719c; -.
DR eggNOG; COG1388; Bacteria.
DR OMA; MTVIHTL; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR InterPro; IPR018392; LysM_dom.
DR Pfam; PF01476; LysM; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall biogenesis/degradation; Hydrolase; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..165
FT /note="Cell wall hydrolase ChiZ"
FT /id="PRO_0000448834"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..163
FT /note="LysM-type"
FT /evidence="ECO:0000305"
SQ SEQUENCE 165 AA; 17324 MW; A02E94DD9586F3CD CRC64;
MTPVRPPHTP DPLNLRGPLD GPRWRRAEPA QSRRPGRSRP GGAPLRYHRT GVGMSRTGHG
SRPVPPATTV GLALLAAAIT LWLGLVAQFG QMITGGSADG SADSTGRVPD RLAVVRVETG
ESLYDVAVRV APNAPTRQVA DRIRELNGLQ TPALAVGQTL IAPVG
