ZIPA_MARN8
ID ZIPA_MARN8 Reviewed; 338 AA.
AC A1TZT8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Cell division protein ZipA {ECO:0000255|HAMAP-Rule:MF_00509};
GN Name=zipA {ECO:0000255|HAMAP-Rule:MF_00509}; OrderedLocusNames=Maqu_1166;
OS Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter
OS aquaeolei).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Marinobacteraceae; Marinobacter.
OX NCBI_TaxID=351348;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700491 / DSM 11845 / VT8;
RX PubMed=21335390; DOI=10.1128/aem.01866-10;
RA Singer E., Webb E.A., Nelson W.C., Heidelberg J.F., Ivanova N., Pati A.,
RA Edwards K.J.;
RT "Genomic potential of Marinobacter aquaeolei, a biogeochemical
RT 'opportunitroph'.";
RL Appl. Environ. Microbiol. 77:2763-2771(2011).
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; CP000514; ABM18257.1; -; Genomic_DNA.
DR RefSeq; WP_011784674.1; NC_008740.1.
DR AlphaFoldDB; A1TZT8; -.
DR SMR; A1TZT8; -.
DR STRING; 351348.Maqu_1166; -.
DR EnsemblBacteria; ABM18257; ABM18257; Maqu_1166.
DR KEGG; maq:Maqu_1166; -.
DR eggNOG; COG3115; Bacteria.
DR HOGENOM; CLU_030174_0_0_6; -.
DR OMA; LDTHKEP; -.
DR OrthoDB; 1632200at2; -.
DR Proteomes; UP000000998; 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 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..338
FT /note="Cell division protein ZipA"
FT /id="PRO_1000060869"
FT TOPO_DOM 1..2
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00509"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00509"
FT TOPO_DOM 24..338
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00509"
FT REGION 33..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 338 AA; 37582 MW; ED410F64F2CF7E36 CRC64;
MSLREWLIAI GTLVIIGIVI DGVRRMRRAR KESMAISSGM GADELKDSPL DDDFNPELPN
GGARTVSRST LEDRGYLKRD MSAPVSTDQE DDVTPESGWS ARDDDEDDGI LSPPRVVKPE
TEESEPVEPE AVKTPATEVD RSKTRPSVPE KAKAEPEPRA EEPPVVTTEV EEDTARRTPN
KPRKNQPLAG ANRPEAREVL VINVLARSGE QFQGSKLKSL FEACGLEQGD MDIYHRHESE
DTTTPVQFSV ANAVEPGTFR PQDMAGLSTP GISFFMSLPG PTNALQAFEF MLETAQCVVR
NLGGELKDER RSVMTPQTIE HCRQRIREFE RKQRSQRA