ID A0A248KH16_9ENTR Unreviewed; 424 AA.
AC A0A248KH16;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 03-MAY-2023, entry version 16.
DE RecName: Full=Cell division protein DamX {ECO:0000256|HAMAP-Rule:MF_02021};
GN Name=damX {ECO:0000256|HAMAP-Rule:MF_02021};
GN ORFNames=CEW81_01980 {ECO:0000313|EMBL:ASG62556.1};
OS Kluyvera genomosp. 3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Kluyvera.
OX NCBI_TaxID=2774055 {ECO:0000313|EMBL:ASG62556.1, ECO:0000313|Proteomes:UP000197098};
RN [1] {ECO:0000313|EMBL:ASG62556.1, ECO:0000313|Proteomes:UP000197098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YDC799 {ECO:0000313|EMBL:ASG62556.1,
RC ECO:0000313|Proteomes:UP000197098};
RA Ito R., Pacey M.P., Doi Y.;
RT "Origin of plasmid-mediated fosfomycin resistance gene fosA3.";
RL Submitted (JUN-2017) 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}.
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DR EMBL; CP022114; ASG62556.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A248KH16; -.
DR KEGG; kgo:CEW81_01980; -.
DR Proteomes; UP000197098; 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 ECO:0000313|EMBL:ASG62556.1};
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:UP000197098};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_02021};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02021}.
FT TRANSMEM 99..120
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02021"
FT DOMAIN 338..415
FT /note="SPOR"
FT /evidence="ECO:0000259|PROSITE:PS51724"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..75
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 424 AA; 45143 MW; 9E66A8D990957363 CRC64;
MDEFKPEDEL KPDPSDRRTG RSRQSSDRDN EPQINFDDVD LDADERRPSR SRKAREEVEP
EDEYEESDEA DEGDAEEVVE RRPRKRKNVA PRKPASRQYI MMGLGVVVLL VLIVGIGSAL
KAPSSNDQSA SGEKSISLSG GDNVDQANVT QSQPAPEANP QQDVSLPPIS STPTQGQQTA
APDGQQRVEV QGDLNNALTQ QQGQIDNAVV NSTLPTEPAT VAPIRNGARP AVTAPETPRQ
TATAPRPERK HTVIEAKPQP VAPAKTQTTT AQSKPAEAKP VTTAPKQTVT AAAPTKAPAA
ETAKPAASTT TPAATAAATA APAAATGKSA GDVGSLKSAS GSHYTLQLSS SSNYDNLNGW
AKKENLKNYV VYETSRNGQP WYVLVSGIYA SKDDAKRAVT TLPADVQAKN PWAKPLHQVQ
SDLK
//