DAMX_ECOLI
ID DAMX_ECOLI Reviewed; 428 AA.
AC P11557; P76687; Q2M753;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Cell division protein DamX {ECO:0000255|HAMAP-Rule:MF_02021, ECO:0000305};
GN Name=damX {ECO:0000255|HAMAP-Rule:MF_02021}; Synonyms=yhfB;
GN OrderedLocusNames=b3388, JW3351;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2549371; DOI=10.1007/bf00330946;
RA Jonczyk P., Hines R., Smith D.W.;
RT "The Escherichia coli dam gene is expressed as a distal gene of a new
RT operon.";
RL Mol. Gen. Genet. 217:85-96(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND OVEREXPRESSION.
RX PubMed=7603433; DOI=10.1007/bf00290345;
RA Lyngstadaas A., Lobner-Olesen A., Boye E.;
RT "Characterization of three genes in the dam-containing operon of
RT Escherichia coli.";
RL Mol. Gen. Genet. 247:546-554(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=19684127; DOI=10.1128/jb.00811-09;
RA Gerding M.A., Liu B., Bendezu F.O., Hale C.A., Bernhardt T.G.,
RA de Boer P.A.;
RT "Self-enhanced accumulation of FtsN at division sites and roles for other
RT proteins with a SPOR domain (DamX, DedD, and RlpA) in Escherichia coli cell
RT constriction.";
RL J. Bacteriol. 191:7383-7401(2009).
RN [6]
RP FUNCTION, INTERACTION WITH FTS PROTEINS, SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=K12 / BW25113;
RX PubMed=19880599; DOI=10.1128/jb.01244-09;
RA Arends S.J., Williams K., Scott R.J., Rolong S., Popham D.L., Weiss D.S.;
RT "Discovery and characterization of three new Escherichia coli septal ring
RT proteins that contain a SPOR domain: DamX, DedD, and RlpA.";
RL J. Bacteriol. 192:242-255(2010).
RN [7]
RP STRUCTURE BY NMR OF 338-428, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS
RP OF GLN-351; SER-354 AND TRP-416.
RX PubMed=23290046; DOI=10.1021/bi301609e;
RA Williams K.B., Yahashiri A., Arends S.J., Popham D.L., Fowler C.A.,
RA Weiss D.S.;
RT "Nuclear magnetic resonance solution structure of the peptidoglycan-binding
RT SPOR domain from Escherichia coli DamX: insights into septal
RT localization.";
RL Biochemistry 52:627-639(2013).
CC -!- FUNCTION: Non-essential cell division protein. {ECO:0000255|HAMAP-
CC Rule:MF_02021, ECO:0000269|PubMed:19684127,
CC ECO:0000269|PubMed:19880599}.
CC -!- SUBUNIT: Interacts in vitro with multiple Fts proteins, including FtsQ
CC and FtsN. {ECO:0000269|PubMed:19880599}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_02021}. Note=Localizes at
CC the septal ring (PubMed:19684127, PubMed:19880599, PubMed:23290046).
CC Recruitment to the septal ring requires FtsZ (PubMed:19880599).
CC {ECO:0000269|PubMed:19684127, ECO:0000269|PubMed:19880599,
CC ECO:0000269|PubMed:23290046}.
CC -!- DOMAIN: The SPOR domain binds septal peptidoglycans and is required to
CC target DamX to the septal ring. {ECO:0000255|HAMAP-Rule:MF_02021,
CC ECO:0000269|PubMed:19880599, ECO:0000269|PubMed:23290046}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant shows no obvious phenotype, but
CC absence of the protein aggravates the division defect in ftsN or dedD
CC mutants. {ECO:0000269|PubMed:19684127}.
CC -!- MISCELLANEOUS: Overexpression induces cell filamentation.
CC {ECO:0000269|PubMed:7603433}.
CC -!- SIMILARITY: Belongs to the DamX family. {ECO:0000255|HAMAP-
CC Rule:MF_02021, ECO:0000305}.
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DR EMBL; X15162; CAA33253.1; -; Genomic_DNA.
DR EMBL; Z19601; CAA79667.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58185.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76413.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77903.1; -; Genomic_DNA.
DR PIR; G65133; Q4ECAD.
DR RefSeq; NP_417847.1; NC_000913.3.
DR RefSeq; WP_000343215.1; NZ_SSZK01000008.1.
DR PDB; 2LFV; NMR; -; A=338-428.
DR PDBsum; 2LFV; -.
DR AlphaFoldDB; P11557; -.
DR BMRB; P11557; -.
DR SMR; P11557; -.
DR BioGRID; 4262961; 603.
DR DIP; DIP-9397N; -.
DR IntAct; P11557; 22.
DR STRING; 511145.b3388; -.
DR jPOST; P11557; -.
DR PaxDb; P11557; -.
DR PRIDE; P11557; -.
DR EnsemblBacteria; AAC76413; AAC76413; b3388.
DR EnsemblBacteria; BAE77903; BAE77903; BAE77903.
DR GeneID; 947930; -.
DR KEGG; ecj:JW3351; -.
DR KEGG; eco:b3388; -.
DR PATRIC; fig|1411691.4.peg.3342; -.
DR EchoBASE; EB1170; -.
DR eggNOG; COG3266; Bacteria.
DR HOGENOM; CLU_048276_1_0_6; -.
DR InParanoid; P11557; -.
DR OMA; ASRQYIM; -.
DR PhylomeDB; P11557; -.
DR BioCyc; EcoCyc:EG11183-MON; -.
DR PHI-base; PHI:6729; -.
DR PRO; PR:P11557; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032153; C:cell division site; IDA:EcoCyc.
DR GO; GO:0030428; C:cell septum; IDA:EcoCyc.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0008047; F:enzyme activator activity; IDA:EcoCyc.
DR GO; GO:0042834; F:peptidoglycan binding; IDA:EcoCyc.
DR GO; GO:0032506; P:cytokinetic process; IEA:InterPro.
DR Gene3D; 3.30.70.1070; -; 1.
DR HAMAP; MF_02021; DamX; 1.
DR InterPro; IPR032899; DamX.
DR InterPro; IPR007730; SPOR-like_dom.
DR InterPro; IPR036680; SPOR-like_sf.
DR Pfam; PF05036; SPOR; 1.
DR SUPFAM; SSF110997; SSF110997; 1.
DR PROSITE; PS51724; SPOR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell inner membrane;
KW Cell membrane; Coiled coil; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..428
FT /note="Cell division protein DamX"
FT /id="PRO_0000079779"
FT TOPO_DOM 1..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23290046"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02021"
FT TOPO_DOM 125..428
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:23290046"
FT DOMAIN 342..419
FT /note="SPOR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02021"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 55..87
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02021"
FT COMPBIAS 1..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..79
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 351
FT /note="Q->K: Eliminates septal localization."
FT /evidence="ECO:0000269|PubMed:23290046"
FT MUTAGEN 354
FT /note="S->K: Impairs septal localization."
FT /evidence="ECO:0000269|PubMed:23290046"
FT MUTAGEN 416
FT /note="W->L: Impairs septal localization."
FT /evidence="ECO:0000269|PubMed:23290046"
FT CONFLICT 6
FT /note="P -> T (in Ref. 1; CAA33253 and 2; CAA79667)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="R -> P (in Ref. 1; CAA33253 and 2; CAA79667)"
FT /evidence="ECO:0000305"
FT CONFLICT 86..91
FT /note="RRPRKR -> LVRVS (in Ref. 1; CAA33253 and 2;
FT CAA79667)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="V -> L (in Ref. 2; CAA79667)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="A -> V (in Ref. 1; CAA33253 and 2; CAA79667)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="K -> N (in Ref. 2; CAA79667)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="G -> V (in Ref. 1; CAA33253 and 2; CAA79667)"
FT /evidence="ECO:0000305"
FT HELIX 358..367
FT /evidence="ECO:0007829|PDB:2LFV"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:2LFV"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:2LFV"
FT HELIX 396..405
FT /evidence="ECO:0007829|PDB:2LFV"
FT HELIX 408..411
FT /evidence="ECO:0007829|PDB:2LFV"
FT TURN 420..422
FT /evidence="ECO:0007829|PDB:2LFV"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:2LFV"
SQ SEQUENCE 428 AA; 46162 MW; E3376F88383BE94A CRC64;
MDEFKPEDEL KPDPSDRRTG RSRQSSERSE RTERGEPQIN FDDIELDDTD DRRPTRAQKE
RNEEPEIEEE IDESEDETVD EERVERRPRK RKKAASKPAS RQYMMMGVGI LVLLLLIIGI
GSALKAPSTT SSDQTASGEK SIDLAGNATD QANGVQPAPG TTSAENTQQD VSLPPISSTP
TQGQTPVATD GQQRVEVQGD LNNALTQPQN QQQLNNVAVN STLPTEPATV APVRNGNASR
DTAKTQTAER PSTTRPARQQ AVIEPKKPQA TVKTEPKPVA QTPKRTEPAA PVASTKAPAA
TSTPAPKETA TTAPVQTASP AQTTATPAAG AKTAGNVGSL KSAPSSHYTL QLSSSSNYDN
LNGWAKKENL KNYVVYETTR NGQPWYVLVS GVYASKEEAK KAVSTLPADV QAKNPWAKPL
RQVQADLK
