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Database: UniProt
Entry: A0A0L0ATD0_9ENTR
LinkDB: A0A0L0ATD0_9ENTR
Original site: A0A0L0ATD0_9ENTR 
ID   A0A0L0ATD0_9ENTR        Unreviewed;       432 AA.
AC   A0A0L0ATD0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Cell division protein DamX {ECO:0000256|HAMAP-Rule:MF_02021};
GN   Name=damX {ECO:0000256|HAMAP-Rule:MF_02021};
GN   ORFNames=AC791_03520 {ECO:0000313|EMBL:KNC11026.1};
OS   Klebsiella sp. RIT-PI-d.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=1681196 {ECO:0000313|EMBL:KNC11026.1, ECO:0000313|Proteomes:UP000053401};
RN   [1] {ECO:0000313|Proteomes:UP000053401}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIT-PI-d {ECO:0000313|Proteomes:UP000053401};
RA   Tan N.E.H., Lee Y.P., Gan H.M., Savka M.A.;
RT   "Whole genome sequencing of endophytes isolated from poison ivy
RT   (Toxicodendron radicans).";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KNC11026.1}.
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DR   EMBL; LGIT01000004; KNC11026.1; -; Genomic_DNA.
DR   RefSeq; WP_049839108.1; NZ_LGIT01000004.1.
DR   AlphaFoldDB; A0A0L0ATD0; -.
DR   STRING; 1681196.AC791_03520; -.
DR   PATRIC; fig|1681196.3.peg.2886; -.
DR   OrthoDB; 6189127at2; -.
DR   Proteomes; UP000053401; Unassembled WGS sequence.
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   ECO:0000313|EMBL:KNC11026.1};
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:UP000053401};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_02021};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02021}.
FT   TRANSMEM        95..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02021"
FT   DOMAIN          346..423
FT                   /note="SPOR"
FT                   /evidence="ECO:0000259|PROSITE:PS51724"
FT   REGION          1..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          116..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          212..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..177
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..233
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..248
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..307
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   432 AA;  46170 MW;  ED69B09F71D09392 CRC64;
     MDEFKPEDEL KPDPSDRRTG RSRQSSDRDN EQQINFDDVE LDADEPRSTR ATRRAREDEE
     YAADDEAFDD EEPVVERRPR KRKKAPASKP ASRQYIMMGV GIVVLLLLIA GIGSALKSPS
     KNESSSTEEK NIALSGNQDT ATQPASDQTA NTAPQDVSLP PISSTPTEGQ APATPDNQQR
     VEVQGDLNNA LTQQQGQVDS AVNSTLPTAP ATVAAVRNGN APRQATTGES TEHRNTTTRP
     ERKQVVIEPK PQSKPQQTAR QTVTEPKTVS QPKRTEATAP VKAPTAEPKA TATRTAPETT
     TPAATAPATS APVAASKPAA TPAPAATAPA ATAGVKSTGN VGSLKSAPSN HYTLQLSSSS
     SYDNLNGWAK KENLKSYVVY QTSRNGQPWY VLVSGVYASK EDAKRAVTAL PADVQAKNPW
     AKPLHQVQAD LK
//
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