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H2A3Q9 (H2A3Q9_STRMD) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 10. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
ATP-dependent zinc metalloprotease FtsH HAMAP-Rule MF_01458

EC=3.4.24.- HAMAP-Rule MF_01458
Gene names
Name:ftsH HAMAP-Rule MF_01458 EMBL CCF01306.1
Ordered Locus Names:SMA_0015 EMBL CCF01306.1
OrganismStreptococcus macedonicus (strain ACA-DC 198) [Complete proteome] [HAMAP] EMBL CCF01306.1
Taxonomic identifier1116231 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length660 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins By similarity. HAMAP-Rule MF_01458

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_01458

Subunit structure

Homohexamer By similarity. HAMAP-Rule MF_01458

Subcellular location

Cell membrane; Multi-pass membrane protein; Cytoplasmic side By similarity HAMAP-Rule MF_01458.

Sequence similarities

In the C-terminal section; belongs to the peptidase M41 family. HAMAP-Rule MF_01458

In the central section; belongs to the AAA ATPase family. HAMAP-Rule MF_01458

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Topological domain1 – 1313Cytoplasmic By similarity HAMAP-Rule MF_01458
Transmembrane14 – 3421Helical; By similarity HAMAP-Rule MF_01458
Topological domain35 – 134100Extracellular By similarity HAMAP-Rule MF_01458
Transmembrane135 – 15521Helical; By similarity HAMAP-Rule MF_01458
Topological domain156 – 660505Cytoplasmic By similarity HAMAP-Rule MF_01458
Nucleotide binding227 – 2348ATP By similarity HAMAP-Rule MF_01458

Sites

Active site4501 By similarity HAMAP-Rule MF_01458
Metal binding4491Zinc; catalytic By similarity HAMAP-Rule MF_01458
Metal binding4531Zinc; catalytic By similarity HAMAP-Rule MF_01458
Metal binding5251Zinc; catalytic By similarity HAMAP-Rule MF_01458

Sequences

Sequence LengthMass (Da)Tools
H2A3Q9 [UniParc].

Last modified March 21, 2012. Version 1.
Checksum: 7A5E1E80A95F30E0

FASTA66071,942
        10         20         30         40         50         60 
MKNNKNNGFV RNSFIYILLI IAGITAFQYY LRGTSTQSQQ INYSTLIKQI KAGDIKSITY 

        70         80         90        100        110        120 
QPSGSIIEVS GEYTKAQTTE TSSSLPFLEG STNSTVTEFT SIVLPSDSSI EAITSAAEDA 

       130        140        150        160        170        180 
DVEVTVKPES SSGTWISYII TYIPFIVLIV FFFVMMNQGG NGARGAMGFG KNRAKFQSKG 

       190        200        210        220        230        240 
NVKVRFSDVA GAEEEKQELV EVVDFLKNPK KYKALGARIP AGVLLEGPPG TGKTLLAKAV 

       250        260        270        280        290        300 
AGEAGVPFFS ISGSDFVEMF VGVGASRVRS LFEDAKKAER AIIFIDEIDA VGRRRGAGMG 

       310        320        330        340        350        360 
GGNDEREQTL NQLLIEMDGF EGNESIIVIA ATNRSDVLDP ALLRPGRFDR KILVGSPDVK 

       370        380        390        400        410        420 
GREAILRVHA KNKPLAEDVN LKVVAQQTPG FVGADLENVL NEAALVAARR NKKKIDASDI 

       430        440        450        460        470        480 
DEAEDRVIAG PSKKDRTISQ KEREMVAYHE AGHTIVGLVL SSARVVHKVT IVPRGRAGGY 

       490        500        510        520        530        540 
MIALPKEDQM LHSKDELKEQ LAGLMGGRVA EEIIFNAQTT GASNDFEQAT QLARAMVTEY 

       550        560        570        580        590        600 
GMSDKLGPVQ YEGNHAVMTG QLSPEKTYSA QTAQMIDDEV RTLLNEARDK AADIINNNRE 

       610        620        630        640        650        660 
THKLIAEALL KYETLNAAQI KSIYETGKMP EELENDTEEA HALSYDEVKE KMDDSDDSKE 

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References

[1]"Complete Genome Sequence of the Dairy Isolate Streptococcus macedonicus ACA-DC 198."
Papadimitriou K., Ferreira S., Papandreou N.C., Mavrogonatou E., Supply P., Pot B., Tsakalidou E.
J. Bacteriol. 194:1838-1839(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ACA-DC 198 EMBL CCF01306.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
HE613569 Genomic DNA. Translation: CCF01306.1.
RefSeqYP_005093756.1. NC_016749.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

MEROPSM41.009.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCF01306; CCF01306; SMA_0015.
GeneID11602596.
KEGGsmn:SMA_0015.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK03798.

Family and domain databases

HAMAPMF_01458. FtsH.
InterProIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR005936. FtsH.
IPR027417. P-loop_NTPase.
IPR011546. Pept_M41_FtsH_extracell.
IPR000642. Peptidase_M41.
[Graphical view]
PfamPF00004. AAA. 1 hit.
PF06480. FtsH_ext. 1 hit.
PF01434. Peptidase_M41. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR01241. FtsH_fam. 1 hit.
PROSITEPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameH2A3Q9_STRMD
AccessionPrimary (citable) accession number: H2A3Q9
Entry history
Integrated into UniProtKB/TrEMBL: March 21, 2012
Last sequence update: March 21, 2012
Last modified: May 29, 2013
This is version 10 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)