CRGA_MYCTU
ID CRGA_MYCTU Reviewed; 93 AA.
AC P9WP57; L0T422; P67376; P71581;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 32.
DE RecName: Full=Cell division protein CrgA {ECO:0000255|HAMAP-Rule:MF_00631};
GN Name=crgA {ECO:0000255|HAMAP-Rule:MF_00631}; OrderedLocusNames=Rv0011c;
GN ORFNames=MTCY10H4.11c;
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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FTSZ; PBPB; FTSQ AND
RP PBPA.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21531798; DOI=10.1128/jb.00188-11;
RA Plocinski P., Ziolkiewicz M., Kiran M., Vadrevu S.I., Nguyen H.B.,
RA Hugonnet J., Veckerle C., Arthur M., Dziadek J., Cross T.A., Madiraju M.,
RA Rajagopalan M.;
RT "Characterization of CrgA, a new partner of the Mycobacterium tuberculosis
RT peptidoglycan polymerization complexes.";
RL J. Bacteriol. 193:3246-3256(2011).
RN [3]
RP FUNCTION, AND INTERACTION WITH CWSA.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=23002219; DOI=10.1128/jb.01005-12;
RA Plocinski P., Arora N., Sarva K., Blaszczyk E., Qin H., Das N.,
RA Plocinska R., Ziolkiewicz M., Dziadek J., Kiran M., Gorla P., Cross T.A.,
RA Madiraju M., Rajagopalan M.;
RT "Mycobacterium tuberculosis CwsA interacts with CrgA and Wag31, and the
RT CrgA-CwsA complex is involved in peptidoglycan synthesis and cell shape
RT determination.";
RL J. Bacteriol. 194:6398-6409(2012).
CC -!- FUNCTION: Involved in cell division. Plays an important role in septal
CC peptidoglycan synthesis and cell shape morphogenesis. May facilitate
CC the recruitment of the peptidoglycan synthesis machinery to poles and
CC septal zones and coordinate peptidoglycan synthesis at these sites.
CC {ECO:0000255|HAMAP-Rule:MF_00631, ECO:0000269|PubMed:21531798,
CC ECO:0000269|PubMed:23002219}.
CC -!- SUBUNIT: Interacts with multiple cell division proteins such as FtsZ,
CC PbpB (PBP3, FtsI), FtsQ, PBPA and CwsA. {ECO:0000269|PubMed:21531798,
CC ECO:0000269|PubMed:23002219}.
CC -!- INTERACTION:
CC P9WP57; P9WJF3: cwsA; NbExp=3; IntAct=EBI-6414478, EBI-6420113;
CC P9WP57; P9WN95: ftsZ; NbExp=5; IntAct=EBI-6414478, EBI-6414519;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00631,
CC ECO:0000269|PubMed:21531798}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00631, ECO:0000269|PubMed:21531798}.
CC Note=Localizes to midcell sites in an FtsZ-dependent manner and
CC colocalizes with FtsZ. Localizes at septa, at poles and on membranes.
CC -!- SIMILARITY: Belongs to the CrgA family. {ECO:0000255|HAMAP-
CC Rule:MF_00631}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL123456; CCP42733.1; -; Genomic_DNA.
DR PIR; A70699; A70699.
DR RefSeq; NP_214525.1; NC_000962.3.
DR RefSeq; WP_003400344.1; NZ_NVQJ01000005.1.
DR PDB; 2MMU; NMR; -; A=1-93.
DR PDBsum; 2MMU; -.
DR AlphaFoldDB; P9WP57; -.
DR BMRB; P9WP57; -.
DR SMR; P9WP57; -.
DR IntAct; P9WP57; 5.
DR STRING; 83332.Rv0011c; -.
DR PaxDb; P9WP57; -.
DR DNASU; 887074; -.
DR GeneID; 45423970; -.
DR GeneID; 887074; -.
DR KEGG; mtu:Rv0011c; -.
DR TubercuList; Rv0011c; -.
DR eggNOG; ENOG5031Y35; Bacteria.
DR OMA; WNIVVGF; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR HAMAP; MF_00631; CrgA; 1.
DR InterPro; IPR009619; CrgA.
DR Pfam; PF06781; CrgA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell membrane; Cell shape;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..93
FT /note="Cell division protein CrgA"
FT /id="PRO_0000216814"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00631"
FT TOPO_DOM 52..69
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00631"
FT TOPO_DOM 91..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT HELIX 31..51
FT /evidence="ECO:0007829|PDB:2MMU"
FT HELIX 71..90
FT /evidence="ECO:0007829|PDB:2MMU"
SQ SEQUENCE 93 AA; 10430 MW; 3D656B59FF629690 CRC64;
MPKSKVRKKN DFTVSAVSRT PMKVKVGPSS VWFVSLFIGL MLIGLIWLMV FQLAAIGSQA
PTALNWMAQL GPWNYAIAFA FMITGLLLTM RWH
