ID D4GCM2_PANAM Unreviewed; 369 AA.
AC D4GCM2;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Cell division protein DamX {ECO:0000256|HAMAP-Rule:MF_02021};
GN Name=damX {ECO:0000256|HAMAP-Rule:MF_02021,
GN ECO:0000313|EMBL:ADD78833.1};
GN OrderedLocusNames=PANA_3666 {ECO:0000313|EMBL:ADD78833.1};
OS Pantoea ananatis (strain LMG 20103).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=706191 {ECO:0000313|EMBL:ADD78833.1, ECO:0000313|Proteomes:UP000001702};
RN [1] {ECO:0000313|EMBL:ADD78833.1, ECO:0000313|Proteomes:UP000001702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 20103 {ECO:0000313|EMBL:ADD78833.1,
RC ECO:0000313|Proteomes:UP000001702};
RX PubMed=20348253; DOI=10.1128/JB.00060-10;
RA De Maayer P., Chan W.Y., Venter S.N., Toth I.K., Birch P.R., Joubert F.,
RA Coutinho T.A.;
RT "Genome sequence of Pantoea ananatis LMG20103, the causative agent of
RT Eucalyptus blight and dieback.";
RL J. Bacteriol. 192:2936-2937(2010).
CC -!- FUNCTION: Non-essential cell division protein. {ECO:0000256|HAMAP-
CC Rule:MF_02021}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_02021}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_02021}. Note=Localizes at the septal ring. {ECO:0000256|HAMAP-
CC Rule:MF_02021}.
CC -!- DOMAIN: The SPOR domain binds septal peptidoglycans and is required to
CC target DamX to the septal ring. {ECO:0000256|HAMAP-Rule:MF_02021}.
CC -!- SIMILARITY: Belongs to the DamX family. {ECO:0000256|HAMAP-
CC Rule:MF_02021}.
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DR EMBL; CP001875; ADD78833.1; -; Genomic_DNA.
DR AlphaFoldDB; D4GCM2; -.
DR STRING; 706191.PANA_3666; -.
DR KEGG; pam:PANA_3666; -.
DR eggNOG; COG3266; Bacteria.
DR HOGENOM; CLU_048276_1_0_6; -.
DR Proteomes; UP000001702; Chromosome.
DR GO; GO:0030428; C:cell septum; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR GO; GO:0032506; P:cytokinetic process; IEA:InterPro.
DR Gene3D; 3.30.70.1070; Sporulation related repeat; 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; Sporulation related repeat; 1.
DR PROSITE; PS51724; SPOR; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_02021};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_02021};
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02021};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_02021};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_02021};
KW Reference proteome {ECO:0000313|Proteomes:UP000001702};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_02021};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02021}.
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02021"
FT DOMAIN 282..359
FT /note="SPOR"
FT /evidence="ECO:0000259|PROSITE:PS51724"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 369 AA; 37447 MW; 83628DD681A3E53F CRC64;
MVTRRAGAQC GMPLYGGGKM DEFKPDDELK PDASDRRPSR PRKSSSATKA PVSRQHVMMG
VGILVLLLLV LGIGSALNGS DDSKSSSASD NKNAPASGAA GTGSEKNIDL SGSTAMSGGQ
NAAGTQPSSS TAQNAPGTDS SAGATNAPRD ISMPPVASTP TQAAPVETPA NQQRVTLPGD
LNSALTNQQQ QVDGAVQGAE NSSSLPTAPA TVSGKAGSAP ATTGRAPSGQ TAVAPRHMRE
QPVKTATRPA ASEHKMHTTP AHTAANTAPA KAAGSGAAAS KSLPGGNYTL QLSGASKAES
LNAWARKQNL SAYHVYKTTR NGQPWYVLVS GAYATPADAK RAVATLPAAV RAQNPWVKPV
SQVRKEASQ
//
