ZIPA_ALISL
ID ZIPA_ALISL Reviewed; 308 AA.
AC B6EJQ7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Cell division protein ZipA {ECO:0000255|HAMAP-Rule:MF_00509};
GN Name=zipA {ECO:0000255|HAMAP-Rule:MF_00509}; OrderedLocusNames=VSAL_I2354;
OS Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS LFI1238)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=316275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LFI1238;
RX PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT LFI1238 shows extensive evidence of gene decay.";
RL BMC Genomics 9:616-616(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; FM178379; CAQ80038.1; -; Genomic_DNA.
DR RefSeq; WP_012550849.1; NC_011312.1.
DR AlphaFoldDB; B6EJQ7; -.
DR SMR; B6EJQ7; -.
DR STRING; 316275.VSAL_I2354; -.
DR EnsemblBacteria; CAQ80038; CAQ80038; VSAL_I2354.
DR KEGG; vsa:VSAL_I2354; -.
DR eggNOG; COG3115; Bacteria.
DR HOGENOM; CLU_030174_1_0_6; -.
DR OMA; FWSIRKQ; -.
DR OrthoDB; 1632200at2; -.
DR Proteomes; UP000001730; Chromosome 1.
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..308
FT /note="Cell division protein ZipA"
FT /id="PRO_1000127214"
FT TOPO_DOM 1..5
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00509"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00509"
FT TOPO_DOM 27..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00509"
FT REGION 43..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 308 AA; 34267 MW; EBCD1F155B284839 CRC64;
MQELRLVLIL VGALAIAALL FHGLWTSRKE TSSKFGKKVD IDFDSESEDE QPTPARGFEQ
PKESVVDVRQ ERKEPAFGRD EPNLSQDPLF DGGTDAILKQ NAEEKEVEPK VIEEPIMTRP
SISESMVKEE PTISFSAIDD VEPTFHKESS VVPAPVEPVI IPEIEPEVVP EPEEDVIVIN
VHGMGNERFN GNRLFNSLEQ NGLIFGDMAI YHRHSDLAGS GKVVFSTANM VAPGHFQVPE
GEEFSTPGIS FFLPLPCNGE ADYNFKLMLQ TAQLVASELG GNVLDEKRNM LTPNKIDEYK
QRVKVFCN