O07621 (HEMAT_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Heme-based aerotactic transducer HemAT

Gene names

Name:	hemAT
Synonyms:	yhfV
Ordered Locus Names:	BSU10380

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	432 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Heme-containing signal transducer responsible for aerotaxis, the migratory response toward or away from oxygen. Ref.3
Subunit structure	Homotetramer Probable. Ref.4
Sequence similarities	Contains 1 methyl-accepting transducer domain.

Ontologies

Keywords
Ligand	Heme Iron Metal-binding
Molecular function	Transducer
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aerotaxis Inferred from direct assay Ref.3. Source: UniProtKB oxygen transport Inferred from electronic annotation. Source: InterPro
Cellular_component	membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	heme binding Inferred from direct assay Ref.3. Source: UniProtKB iron ion binding Inferred from electronic annotation. Source: InterPro oxygen binding Inferred from electronic annotation. Source: InterPro signal transducer activity Inferred from direct assay Ref.3. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 432

432

Heme-based aerotactic transducer HemAT

PRO_0000110567

Regions

Domain

184 – 420

237

Methyl-accepting transducer

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

432

Helix Strand Turn

Details...

Helix

18 – 21

4

Helix

29 – 31

3

Helix

32 – 40

9

Helix

45 – 73

29

Helix

77 – 86

10

Helix

89 – 102

14

Helix

110 – 125

16

Helix

130 – 151

22

Helix

155 – 176

22

Sequences

	Sequence		Length	Mass (Da)
	O07621 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 87D0655974070B64	FASTA	432	48,767
	10 20 30 40 50 60 MLFKKDRKQE TAYFSDSNGQ QKNRIQLTNK HADVKKQLKM VRLGDAELYV LEQLQPLIQE 70 80 90 100 110 120 NIVNIVDAFY KNLDHESSLM DIINDHSSVD RLKQTLKRHI QEMFAGVIDD EFIEKRNRIA 130 140 150 160 170 180 SIHLRIGLLP KWYMGAFQEL LLSMIDIYEA SITNQQELLK AIKATTKILN LEQQLVLEAF 190 200 210 220 230 240 QSEYNQTRDE QEEKKNLLHQ KIQETSGSIA NLFSETSRSV QELVDKSEGI SQASKAGTVT 250 260 270 280 290 300 SSTVEEKSIG GKKELEVQQK QMNKIDTSLV QIEKEMVKLD EIAQQIEKIF GIVTGIAEQT 310 320 330 340 350 360 NLLSLNASIE SARAGEHGKG FAVVANEVRK LSEDTKKTVS TVSELVNNTN TQINIVSKHI 370 380 390 400 410 420 KDVNELVSES KEKMTQINRL FDEIVHSMKI SKEQSGKIDV DLQAFLGGLQ EVSRAVSHVA 430 ASVDSLVILT EE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus subtilis chromosome contains several dysfunctional genes, the glyB marker, many genes encoding transporter proteins, and the ubiquitous hit gene." Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H., Venema G., Bron S. Microbiology 144:859-875(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Myoglobin-like aerotaxis transducers in Archaea and Bacteria." Hou S., Larsen R.W., Boudko D., Riley C.W., Karatan E., Zimmer M., Ordal G.W., Alam M. Nature 403:540-544(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[4]	"Resonance Raman and ligand binding studies of the oxygen-sensing signal transducer protein HemAT from Bacillus subtilis." Aono S., Kato T., Matsuki M., Nakajima H., Ohta T., Uchida T., Kitagawa T. J. Biol. Chem. 277:13528-13538(2002) [PubMed] [Europe PMC] [Abstract] Cited for: RESONANCE RAMAN SPECTROSCOPY, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y14084 Genomic DNA. Translation: CAA74545.1.
AL009126 Genomic DNA. Translation: CAB12878.1.

PIR

C69832.

RefSeq

NP_388919.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OR4	X-ray	2.15	A/B	1-178	[»]
1OR6	X-ray	2.71	A/B	1-178	[»]

ProteinModelPortal

O07621.

SMR

O07621. Positions 10-178, 209-412.

ModBase

Search...

Protein-protein interaction databases

IntAct

O07621. 2 interactions.

STRING

224308.BSU10380.

Proteomic databases

PaxDb

O07621.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB12878; CAB12878; BSU10380.

GeneID

936320.

KEGG

bsu:BSU10380.

PATRIC

18973778. VBIBacSub10457_1083.

Organism-specific databases

GenoList

BSU10380. [Micado]

Phylogenomic databases

eggNOG

COG0840.

HOGENOM

HOG000099831.

KO

K06595.

OMA

DHESSLM.

ProtClustDB

CLSK2393374.

Enzyme and pathway databases

BioCyc

BSUB:BSU10380-MONOMER.

Family and domain databases

Gene3D

1.10.490.10. 1 hit.

InterPro

IPR009050. Globin-like.
IPR012292. Globin_dom.
IPR004089. MCPsignal_dom.
[Graphical view]

Pfam

PF00015. MCPsignal. 1 hit.
[Graphical view]

SMART

SM00283. MA. 1 hit.
[Graphical view]

SUPFAM

SSF46458. Globin_like. 1 hit.

PROSITE

PS50111. CHEMOTAXIS_TRANSDUC_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O07621.

Entry information

Entry name

HEMAT_BACSU

Accession

Primary (citable) accession number: O07621

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	July 1, 1997
Last modified:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program