UniProtKB - P77173 (ZIPA_ECOLI)

BLAST

>sp|P77173|ZIPA_ECOLI Cell division protein ZipA OS=Escherichia coli (strain K12) OX=83333 GN=zipA PE=1 SV=3
MMQDLRLILIIVGAIAIIALLVHGFWTSRKERSSMFRDRPLKRMKSKRDDDSYDEDVEDD
EGVGEVRVHRVNHAPANAQEHEAARPSPQHQYQPPYASAQPRQPVQQPPEAQVPPQHAPH
PAQPVQQPAYQPQPEQPLQQPVSPQVAPAPQPVHSAPQPAQQAFQPAEPVAAPQPEPVAE
PAPVMDKPKRKEAVIIMNVAAHHGSELNGELLLNSIQQAGFIFGDMNIYHRHLSPDGSGP
ALFSLANMVKPGTFDPEMKDFTTPGVTIFMQVPSYGDELQNFKLMLQSAQHIADEVGGVV
LDDQRRMMTPQKLREYQDIIREVKDANA

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History
Entry version 144 (07 Nov 2018)
Sequence version 3 (29 Aug 2003)
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Protein

Cell division protein ZipA

Gene

zipA

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring (PubMed:9008158, PubMed:11847116, PubMed:22164258, PubMed:22304478, PubMed:23233671). Also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL and FtsN (PubMed:11847116, PubMed:11948172). ZipA overproduction protects FtsZ from degradation by ClpP by preventing recognition by ClpX (PubMed:23233671). Does not affect the GTPase activity of FtsZ (PubMed:10209756).7 Publications

Miscellaneous

Has been isolated as a 91 kDa complex containing ZipA-EptA and an unidentified 24 kDa protein (PubMed:16079137), but it was shown later that there is no physical interaction between ZipA and EptA (PubMed:22304478).2 Publications

GO - Biological processⁱ

division septum assembly
Source: EcoliWiki
Inferred from mutant phenotypeⁱ
- 9008158
FtsZ-dependent cytokinesis Source: UniProtKB-UniRule

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Biological process	Cell cycle, Cell division

Biological process

Cell cycle, Cell division

Enzyme and pathway databases

BioCycⁱ	EcoCyc:G7258-MONOMER

BioCycⁱ

EcoCyc:G7258-MONOMER

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Cell division protein ZipAUniRule annotation Alternative name(s): FtsZ interacting protein A1 Publication
Gene namesⁱ	Name:zipA1 PublicationUniRule annotation Ordered Locus Names:b2412, JW2404
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG14169 zipA

EcoGeneⁱ

EG14169 zipA

Subcellular locationⁱ

Cell inner membrane
2 Publications
Manual assertion based on experiment inⁱ
- Ref.1
  "Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli."
  Hale C.A., de Boer P.A.J.
  Cell 88:175-185(1997) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH FTSZ, SUBCELLULAR LOCATION, TOPOLOGY.
- Ref.10
  "Protein complexes of the Escherichia coli cell envelope."
  Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
  J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION.
; Single-pass type I membrane protein
1 Publication
Manual assertion based on experiment inⁱ
- Ref.1
  "Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli."
  Hale C.A., de Boer P.A.J.
  Cell 88:175-185(1997) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH FTSZ, SUBCELLULAR LOCATION, TOPOLOGY.

Note:

Localizes to the Z ring in an FtsZ-dependent manner (PubMed:9008158, PubMed:9864327, PubMed:10209756). Localization does not depend upon FtsA or FtsI (PubMed:9864327, PubMed:10209756).3 Publications

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 6	PeriplasmicUniRule annotation1 Publication	6
Transmembraneⁱ	7 – 27	HelicalUniRule annotationAdd BLAST	21
Topological domainⁱ	28 – 328	CytoplasmicUniRule annotation1 PublicationAdd BLAST	301

GO - Cellular componentⁱ

cell division site
Source: EcoliWiki
Inferred from direct assayⁱ
- 9008158
integral component of plasma membrane
Source: EcoliWiki
Inferred from direct assayⁱ
- 9008158
plasma membrane
Source: EcoCyc
Inferred from direct assayⁱ
- 17309111

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechⁱ

Chemistry databases

ChEMBLⁱ	CHEMBL3954
Drug and drug target database More...DrugBankⁱ	DB03916 4-{2-[4-(2-Aminoethyl)Piperazin-1-Yl]Pyridin-4-Yl}-N-(3-Chloro-4-Methylphenyl)Pyrimidin-2-Amine

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000214521	1 – 328	Cell division protein ZipAAdd BLAST		328

Proteomic databases

PaxDbⁱ	P77173
PRIDEⁱ	P77173

Expressionⁱ

Inductionⁱ

Repressed 1.5-fold by hydroxyurea.1 Publication

Interactionⁱ

Subunit structureⁱ

Interacts with FtsZ via their C-terminal domains (PubMed:9008158, PubMed:10209756, PubMed:10880432, PubMed:22164258). Can form homodimers prior to association with FtsZ (PubMed:22304478).5 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
ftsZ	P0A9A6	5	EBI-1029213,EBI-370963

With

Entry

#Exp.

IntAct

Notes

ftsZ

P0A9A6

EBI-1029213,EBI-370963

Protein-protein interaction databases

BioGridⁱ	4261708, 561 interactors
Database of interacting proteins More...DIPⁱ	DIP-1157N
IntActⁱ	P77173, 2 interactors
STRINGⁱ	316385.ECDH10B_2577

Chemistry databases

BindingDBⁱ

P77173

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	193 – 200	Combined sources	8
Helixⁱ	209 – 218	Combined sources	10
Beta strandⁱ	221 – 223	Combined sources	3
Helixⁱ	225 – 227	Combined sources	3
Beta strandⁱ	228 – 234	Combined sources	7
Beta strandⁱ	241 – 249	Combined sources	9
Turnⁱ	256 – 259	Combined sources	4
Beta strandⁱ	262 – 272	Combined sources	11
Beta strandⁱ	274 – 276	Combined sources	3
Helixⁱ	278 – 296	Combined sources	19
Beta strandⁱ	299 – 301	Combined sources	3
Beta strandⁱ	305 – 307	Combined sources	3
Helixⁱ	310 – 326	Combined sources	17

Show more details

3D structure databases

Database of protein disorder More...DisProtⁱ	DP00161
ProteinModelPortalⁱ	P77173
SMRⁱ	P77173
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P77173

Family & Domainsⁱ

Domainⁱ

Contains an N-terminal transmembrane domain, followed by a charged domain, an unstructured P/Q domain rich in proline and glutamine, and a C-terminal FtsZ-binding domain.1 Publication

Sequence similaritiesⁱ

Belongs to the ZipA family.UniRule annotationCurated

Keywords - Domainⁱ

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	ENOG4107NPY Bacteria COG3115 LUCA
HOGENOMⁱ	HOG000274007
InParanoidⁱ	P77173
KEGG Orthology (KO) More...KOⁱ	K03528

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00231 ZipA, 1 hit
Gene3Dⁱ	3.30.1400.10, 1 hit
HAMAPⁱ	MF_00509 ZipA, 1 hit
InterProⁱ	View protein in InterPro IPR011919 Cell_div_ZipA IPR007449 ZipA_FtsZ-bd_C IPR036765 ZipA_FtsZ-bd_C_sf
PANTHERⁱ	PTHR38685 PTHR38685, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF04354 ZipA_C, 1 hit
ProDomⁱ	View protein in ProDom or Entries sharing at least one domain PD035754 ZipA_Fts_Z_bd_C, 1 hit
SMARTⁱ	View protein in SMART SM00771 ZipA_C, 1 hit
SUPFAMⁱ	SSF64383 SSF64383, 1 hit
TIGRFAMsⁱ	TIGR02205 septum_zipA, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P77173-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MMQDLRLILI IVGAIAIIAL LVHGFWTSRK ERSSMFRDRP LKRMKSKRDD 
        60         70         80         90        100
DSYDEDVEDD EGVGEVRVHR VNHAPANAQE HEAARPSPQH QYQPPYASAQ 
       110        120        130        140        150
PRQPVQQPPE AQVPPQHAPH PAQPVQQPAY QPQPEQPLQQ PVSPQVAPAP 
       160        170        180        190        200
QPVHSAPQPA QQAFQPAEPV AAPQPEPVAE PAPVMDKPKR KEAVIIMNVA 
       210        220        230        240        250
AHHGSELNGE LLLNSIQQAG FIFGDMNIYH RHLSPDGSGP ALFSLANMVK 
       260        270        280        290        300
PGTFDPEMKD FTTPGVTIFM QVPSYGDELQ NFKLMLQSAQ HIADEVGGVV 
       310        320 
LDDQRRMMTP QKLREYQDII REVKDANA

Length:328

Mass (Da):36,475

Last modified:August 29, 2003 - v3

Checksum:ⁱA20F119A153A782B

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	211	L → A in AAB42061 (PubMed:9008158).Curated		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U74650 Genomic DNA Translation: AAB42061.1 U00096 Genomic DNA Translation: AAC75465.1 AP009048 Genomic DNA Translation: BAA16284.1
PIRⁱ	C65015
NCBI Reference Sequences More...RefSeqⁱ	NP_416907.1, NC_000913.3 WP_001300494.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC75465; AAC75465; b2412 BAA16284; BAA16284; BAA16284
GeneIDⁱ	946869
KEGGⁱ	ecj:JW2404 eco:b2412
PATRICⁱ	fig\|511145.12.peg.2506

Protein	Similar proteins		Species	Score	Length	Source
P77173	Cell division protein ZipA		ECOBW		328	UniRef100_C4ZVU3
Cell division protein ZipA		ECODH		328
Cell division protein ZipA		ECOLC		328
Cell division protein ZipA		Escherichia coli H736		345
Cell division protein ZipA		Escherichia coli H386		345
+15

Protein	Similar proteins		Species	Score	Length	Source
P77173	Cell division protein ZipA		ECOL6		332	UniRef90_Q8FFC0
Cell division protein ZipA		ECO45		332
Cell division protein ZipA		ECOK1		332
Cell division protein ZipA		ECOSM		332
Cell division protein ZipA		ECOUT		332
+747

Protein	Similar proteins		Species	Score	Length	Source
P77173	Cell division protein ZipA		ECOL6		332	UniRef50_Q8FFC0
Cell division protein ZipA		ECO5E		332
Cell division protein ZipA		SHIDS		332
Cell division protein ZipA		ECO27		332
Cell division protein ZipA		ECO45		332
+1580

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U74650 Genomic DNA Translation: AAB42061.1 U00096 Genomic DNA Translation: AAC75465.1 AP009048 Genomic DNA Translation: BAA16284.1
PIRⁱ	C65015
RefSeqⁱ	NP_416907.1, NC_000913.3 WP_001300494.1, NZ_LN832404.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1F46	X-ray	1.50	A/B	189-328	[»]
	1F47	X-ray	1.95	B	185-328	[»]
	1F7W	NMR	-	A	185-328	[»]
	1F7X	NMR	-	A	185-328	[»]
	1S1J	X-ray	2.18	A/B	185-328	[»]
	1S1S	X-ray	2.10	A/B	185-328	[»]
	1Y2F	X-ray	2.00	A	190-328	[»]
	1Y2G	X-ray	1.90	A/B	189-328	[»]
DisProtⁱ	DP00161
ProteinModelPortalⁱ	P77173
SMRⁱ	P77173
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4261708, 561 interactors
DIPⁱ	DIP-1157N
IntActⁱ	P77173, 2 interactors
STRINGⁱ	316385.ECDH10B_2577

Chemistry databases

BindingDBⁱ	P77173
ChEMBLⁱ	CHEMBL3954
DrugBankⁱ	DB03916 4-{2-[4-(2-Aminoethyl)Piperazin-1-Yl]Pyridin-4-Yl}-N-(3-Chloro-4-Methylphenyl)Pyrimidin-2-Amine

Proteomic databases

PaxDbⁱ	P77173
PRIDEⁱ	P77173

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC75465; AAC75465; b2412 BAA16284; BAA16284; BAA16284
GeneIDⁱ	946869
KEGGⁱ	ecj:JW2404 eco:b2412
PATRICⁱ	fig\|511145.12.peg.2506

Organism-specific databases

EchoBASEⁱ	EB3921
EcoGeneⁱ	EG14169 zipA

Phylogenomic databases

eggNOGⁱ	ENOG4107NPY Bacteria COG3115 LUCA
HOGENOMⁱ	HOG000274007
InParanoidⁱ	P77173
KOⁱ	K03528

Enzyme and pathway databases

BioCycⁱ	EcoCyc:G7258-MONOMER

BioCycⁱ

EcoCyc:G7258-MONOMER

Miscellaneous databases

EvolutionaryTraceⁱ	P77173
Protein Ontology More...PROⁱ	PR:P77173

Family and domain databases

CDDⁱ	cd00231 ZipA, 1 hit
Gene3Dⁱ	3.30.1400.10, 1 hit
HAMAPⁱ	MF_00509 ZipA, 1 hit
InterProⁱ	View protein in InterPro IPR011919 Cell_div_ZipA IPR007449 ZipA_FtsZ-bd_C IPR036765 ZipA_FtsZ-bd_C_sf
PANTHERⁱ	PTHR38685 PTHR38685, 1 hit
Pfamⁱ	View protein in Pfam PF04354 ZipA_C, 1 hit
ProDomⁱ	View protein in ProDom or Entries sharing at least one domain PD035754 ZipA_Fts_Z_bd_C, 1 hit
SMARTⁱ	View protein in SMART SM00771 ZipA_C, 1 hit
SUPFAMⁱ	SSF64383 SSF64383, 1 hit
TIGRFAMsⁱ	TIGR02205 septum_zipA, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ZIPA_ECOLI
Accessionⁱ	P77173Primary (citable) accession number: P77173
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
	Last sequence update:	August 29, 2003
	Last modified:	November 7, 2018
	This is version 144 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

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Supporting data

UniProtKB - P77173 (ZIPA_ECOLI)

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Cell division protein ZipA

zipA

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

GO - Cellular componenti

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ