ZIPA_KLEP3
ID ZIPA_KLEP3 Reviewed; 354 AA.
AC B5XVT3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Cell division protein ZipA {ECO:0000255|HAMAP-Rule:MF_00509};
GN Name=zipA {ECO:0000255|HAMAP-Rule:MF_00509}; OrderedLocusNames=KPK_1380;
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342;
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(2008).
CC -!- FUNCTION: Essential cell division protein that stabilizes the FtsZ
CC protofilaments by cross-linking them and that serves as a cytoplasmic
CC membrane anchor for the Z ring. Also required for the recruitment to
CC the septal ring of downstream cell division proteins.
CC {ECO:0000255|HAMAP-Rule:MF_00509}.
CC -!- SUBUNIT: Interacts with FtsZ via their C-terminal domains.
CC {ECO:0000255|HAMAP-Rule:MF_00509}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00509}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00509}. Note=Localizes to the Z ring in an FtsZ-dependent
CC manner. {ECO:0000255|HAMAP-Rule:MF_00509}.
CC -!- SIMILARITY: Belongs to the ZipA family. {ECO:0000255|HAMAP-
CC Rule:MF_00509}.
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DR EMBL; CP000964; ACI07365.1; -; Genomic_DNA.
DR AlphaFoldDB; B5XVT3; -.
DR SMR; B5XVT3; -.
DR PRIDE; B5XVT3; -.
DR EnsemblBacteria; ACI07365; ACI07365; KPK_1380.
DR KEGG; kpe:KPK_1380; -.
DR HOGENOM; CLU_030174_1_0_6; -.
DR OMA; FWSIRKQ; -.
DR Proteomes; UP000001734; Chromosome.
DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0090529; P:cell septum assembly; IEA:InterPro.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR CDD; cd00231; ZipA; 1.
DR Gene3D; 3.30.1400.10; -; 1.
DR HAMAP; MF_00509; ZipA; 1.
DR InterPro; IPR011919; Cell_div_ZipA.
DR InterPro; IPR007449; ZipA_FtsZ-bd_C.
DR InterPro; IPR036765; ZipA_FtsZ-bd_C_sf.
DR PANTHER; PTHR38685; PTHR38685; 1.
DR Pfam; PF04354; ZipA_C; 1.
DR SMART; SM00771; ZipA_C; 1.
DR SUPFAM; SSF64383; SSF64383; 1.
DR TIGRFAMs; TIGR02205; septum_zipA; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; Membrane;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..354
FT /note="Cell division protein ZipA"
FT /id="PRO_1000127221"
FT TOPO_DOM 1..6
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00509"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00509"
FT TOPO_DOM 28..354
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00509"
FT REGION 41..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..208
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 354 AA; 39403 MW; 9CDEC163FD9295F2 CRC64;
MMQDLRLILI IVGAIAIIAL LVHGFWTSRK ERSSMFRDRP LKRMKSRDDE SENEDFDDNV
EGVGEVRVHP VTHAPHGAHG EHEAPRQAPQ HQYQPPYERQ MQQPVRPDEP VRQPQQSPRQ
APVQPQGQQP VPHAAPQPGW QQPQPAQPPV QPQHQPQPVV QQPVAPQPVT PTVAQPQPAA
PQQPVPQPVA APQPAVAEPQ PVEPQQPAAP QPKERKETVI VMNVAAHHGA QLNGEVLINS
IQQAGFKFGE MNIFHRHLSP DGSGPVLFSL ANMVKPGTFN PDSMADMMTP GVTIFMQVPS
YGDELQNFKL MLQSAQYIAD EVGGVVLDDQ RRMMTPQKLR EYQDRIREVK DANA