P28366 (SECA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein translocase subunit SecA

Gene names

Name:	secA
Synonyms:	div+
Ordered Locus Names:	BSU35300

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	841 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane By similarity. HAMAP MF_01382
Cofactor	May bind 1 zinc ion per subunit Potential.
Subunit structure	Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF. Other proteins may be involved. Monomer and many different homodimers can be isolated (Ref.7), some of which are not formed in the presence of a synthetic signal peptide. A single SecA monomer interacts with SecY in the channel.
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasm. Note: Distribution is 50-50 By similarity. HAMAP MF_01382
Sequence similarities	Belongs to the SecA family.

Ontologies

Keywords
Biological process	Protein transport Translocation Transport
Cellular component	Cell membrane Cytoplasm Membrane
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein import Inferred from electronic annotation. Source: InterPro protein targeting Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW helicase activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleic acid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 841

841

Protein translocase subunit SecA HAMAP MF_01382

PRO_0000109576

Regions

Nucleotide binding

100 – 107

8

ATP Potential

Sites

Metal binding

825

1

Zinc Potential

Metal binding

827

1

Zinc Potential

Metal binding

836

1

Zinc Potential

Metal binding

837

1

Zinc Potential

Experimental info

Mutagenesis

587

1

G → C: Forms position 587-750 dimers upon oxidation in vitro; when associated with C-750. Does not form position 587-587 dimers (homodimers). Ref.7

Mutagenesis

588

1

N → C: Forms position 588-588 dimers upon oxidation in vitro (homodimers). Ref.7

Mutagenesis

750

1

R → C: Forms position 587-750 dimers upon oxidation in vitro; when associated with C-587. Also forms position 750-750 dimers (homodimers). Ref.7

Sequence conflict

126

1

V → I in CAA43977. Ref.4

Secondary structure

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841

Helix Strand Turn

Details...

Helix

1 – 6

6

Helix

18 – 28

11

Helix

31 – 34

4

Helix

38 – 53

16

Helix

58 – 77

20

Helix

83 – 93

11

Beta strand

96 – 99

4

Helix

106 – 118

13

Beta strand

124 – 130

7

Helix

131 – 147

17

Beta strand

152 – 154

3

Helix

161 – 169

9

Beta strand

170 – 176

7

Helix

177 – 187

11

Helix

193 – 195

3

Beta strand

203 – 207

5

Helix

209 – 213

5

Turn

214 – 218

5

Beta strand

220 – 228

9

Helix

232 – 241

10

Beta strand

246 – 250

5

Beta strand

254 – 256

3

Helix

263 – 272

10

Helix

281 – 283

3

Helix

284 – 298

15

Turn

302 – 304

3

Beta strand

305 – 309

5

Beta strand

312 – 316

5

Turn

318 – 320

3

Helix

333 – 340

8

Beta strand

349 – 356

8

Helix

357 – 361

5

Beta strand

364 – 372

9

Helix

375 – 377

3

Helix

378 – 385

8

Beta strand

389 – 391

3

Beta strand

406 – 410

5

Helix

411 – 427

17

Beta strand

432 – 437

6

Helix

439 – 450

12

Turn

451 – 453

3

Beta strand

457 – 459

3

Helix

464 – 471

8

Turn

472 – 475

4

Beta strand

480 – 484

5

Helix

500 – 502

3

Beta strand

504 – 511

8

Helix

516 – 523

8

Helix

528 – 530

3

Beta strand

533 – 540

8

Helix

545 – 547

3

Helix

550 – 561

12

Beta strand

565 – 567

3

Helix

572 – 618

47

Helix

624 – 641

18

Helix

657 – 662

6

Turn

663 – 665

3

Beta strand

672 – 675

4

Helix

681 – 702

22

Helix

707 – 736

30

Helix

738 – 740

3

Beta strand

744 – 746

3

Helix

748 – 776

29

Beta strand

794 – 797

4

Sequences

	Sequence		Length	Mass (Da)
	P28366 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: 9AAC3630139F5EFF	FASTA	841	95,531
	10 20 30 40 50 60 MLGILNKMFD PTKRTLNRYE KIANDIDAIR GDYENLSDDA LKHKTIEFKE RLEKGATTDD 70 80 90 100 110 120 LLVEAFAVVR EASRRVTGMF PFKVQLMGGV ALHDGNIAEM KTGEGKTLTS TLPVYLNALT 130 140 150 160 170 180 GKGVHVVTVN EYLASRDAEQ MGKIFEFLGL TVGLNLNSMS KDEKREAYAA DITYSTNNEL 190 200 210 220 230 240 GFDYLRDNMV LYKEQMVQRP LHFAVIDEVD SILIDEARTP LIISGQAAKS TKLYVQANAF 250 260 270 280 290 300 VRTLKAEKDY TYDIKTKAVQ LTEEGMTKAE KAFGIDNLFD VKHVALNHHI NQALKAHVAM 310 320 330 340 350 360 QKDVDYVVED GQVVIVDSFT GRLMKGRRYS EGLHQAIEAK EGLEIQNESM TLATITFQNY 370 380 390 400 410 420 FRMYEKLAGM TGTAKTEEEE FRNIYNMQVV TIPTNRPVVR DDRPDLIYRT MEGKFKAVAE 430 440 450 460 470 480 DVAQRYMTGQ PVLVGTVAVE TSELISKLLK NKGIPHQVLN AKNHEREAQI IEEAGQKGAV 490 500 510 520 530 540 TIATNMAGRG TDIKLGEGVK ELGGLAVVGT ERHESRRIDN QLRGRSGRQG DPGITQFYLS 550 560 570 580 590 600 MEDELMRRFG AERTMAMLDR FGMDDSTPIQ SKMVSRAVES SQKRVEGNNF DSRKQLLQYD 610 620 630 640 650 660 DVLRQQREVI YKQRFEVIDS ENLREIVENM IKSSLERAIA AYTPREELPE EWKLDGLVDL 670 680 690 700 710 720 INTTYLDEGA LEKSDIFGKE PDEMLELIMD RIITKYNEKE EQFGKEQMRE FEKVIVLRAV 730 740 750 760 770 780 DSKWMDHIDA MDQLRQGIHL RAYAQTNPLR EYQMEGFAMF EHMIESIEDE VAKFVMKAEI 790 800 810 820 830 840 ENNLEREEVV QGQTTAHQPQ EGDDNKKAKK APVRKVVDIG RNAPCHCGSG KKYKNCCGRT E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequencing reveals similarity of the wild-type div+ gene of Bacillus subtilis to the Escherichia coli secA gene." Sadaie Y., Takamatsu H., Nakamura K., Yamane K. Gene 98:101-105(1991) [PubMed: 1901557] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
[2]	"Sequence of the 305 degrees-307 degrees region of the Bacillus subtilis chromosome." Soldo B., Lazarevic V., Mauel C., Karamata D. Microbiology 142:3079-3088(1996) [PubMed: 8969505] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"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: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"Identification of a gene fragment which codes for the 364 amino-terminal amino acid residues of a SecA homologue from Bacillus subtilis: further evidence for the conservation of the protein export apparatus in Gram-positive and Gram-negative bacteria." Overhoff B., Klein M., Spies M., Freudl R. Mol. Gen. Genet. 228:417-423(1991) [PubMed: 1832735] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-364.
[5]	"Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA." Hunt J.F., Weinkauf S., Henry L., Fak J.J., McNicholas P., Oliver D.B., Deisenhofer J. Science 297:2018-2026(2002) [PubMed: 12242434] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-802 (MONOMERIC AND DIMERIC) WITH AND WITHOUT BOUND ADP.
[6]	"A large conformational change of the translocation ATPase SecA." Osborne A.R., Clemons W.M. Jr., Rapoport T.A. Proc. Natl. Acad. Sci. U.S.A. 101:10937-10942(2004) [PubMed: 15256599] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF OPEN MONOMERIC SECA.
[7]	"A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecA." Zimmer J., Li W., Rapoport T.A. J. Mol. Biol. 364:259-265(2006) [PubMed: 16989859] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1-780 IN A DIMERIC FORM, STUDY OF DIMERIC FORMS, MUTAGENESIS OF GLY-587; ASN-588 AND ARG-750.
[8]	"Structure of a complex of the ATPase SecA and the protein-translocation channel." Zimmer J., Nam Y., Rapoport T.A. Nature 455:936-943(2008) [PubMed: 18923516] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (7.5 ANGSTROMS) OF 1-779 IN COMPLEX WITH SECYEG FROM A.AEOLICUS.
[9]	"Conformational flexibility and peptide interaction of the translocation ATPase SecA." Zimmer J., Rapoport T.A. J. Mol. Biol. 394:606-612(2009) [PubMed: 19850053] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-780.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D10279 Genomic DNA. Translation: BAA01122.1.
U56901 Genomic DNA. Translation: AAC44957.1.
AL009126 Genomic DNA. Translation: CAB15547.1.
X62035 Genomic DNA. Translation: CAA43977.1.

PIR

JQ0647.

RefSeq

NP_391410.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M6N	X-ray	2.70	A	1-802	[»]
1M74	X-ray	3.00	A	1-802	[»]
1TF2	X-ray	2.90	A	1-841	[»]
1TF5	X-ray	2.18	A	1-841	[»]
2IBM	X-ray	3.20	A/B	1-780	[»]
3DL8	X-ray	7.50	A/B	1-779	[»]
3IQM	X-ray	3.40	A	1-802	[»]
3IQY	X-ray	3.30	A	1-841	[»]
3JV2	X-ray	2.50	A/B	1-780	[»]

ProteinModelPortal

P28366.

SMR

P28366. Positions 1-802.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBBACT00000000374; EBBACP00000000374; EBBACG00000000372.

GeneID

936711.

GenomeReviews

Gene locus BSU35300 in contig AL009126_GR.

KEGG

bsu:BSU35300.

NMPDR

fig|224308.1.peg.3536.

PATRIC

18979066. VBIBacSub10457_3695.

Organism-specific databases

GenoList

BSU35300. [Micado]

Phylogenomic databases

GeneTree

EBGT00050000002757.

HOGENOM

HBG284200.

OMA

GGMVLHD.

PhylomeDB

P28366.

ProtClustDB

PRK12904.

Enzyme and pathway databases

BioCyc

BSUB:BSU35300-MONOMER.

Family and domain databases

HAMAP

MF_01382. SecA.
[Tree]

InterPro

IPR001650. Helicase_C.
IPR004027. SEC_C_motif.
IPR000185. SecA.
IPR020937. SecA_CS.
IPR011115. SecA_DEAD.
IPR014018. SecA_motor_DEAD.
IPR011130. SecA_preprotein_X-link_dom.
IPR011116. SecA_Wing/Scaffold.
[Graphical view]

Gene3D

G3DSA:3.90.1440.10. G3DSA:3.90.1440.10. 1 hit.
G3DSA:1.10.3060.10. SecA_SW. 1 hit.

KO

K03070.

Pfam

PF00271. Helicase_C. 1 hit.
PF02810. SEC-C. 1 hit.
PF07517. SecA_DEAD. 1 hit.
PF01043. SecA_PP_bind. 1 hit.
PF07516. SecA_SW. 1 hit.
[Graphical view]

PRINTS

PR00906. SECA.

SMART

SM00957. SecA_DEAD. 1 hit.
SM00958. SecA_PP_bind. 1 hit.
[Graphical view]

SUPFAM

SSF81767. SecA_PP_bd. 1 hit.
SSF81886. SecA_SW. 1 hit.

TIGRFAMs

TIGR00963. SecA. 1 hit.

PROSITE

PS01312. SECA. 1 hit.
PS51196. SECA_MOTOR_DEAD. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SECA_BACSU

Accession

Primary (citable) accession number: P28366

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	January 25, 2012
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program