Reviewed, UniProtKB/Swiss-Prot P43803 (SECA_HAEIN)

Names and origin

Protein names

Recommended name:
    Protein translocase subunit secA

Gene names

Name:	secA
Ordered Locus Names:	HI0909

Organism

Haemophilus influenzae [Complete proteome] [HAMAP]

Taxonomic identifier

727 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	901 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 both as a receptor for the preprotein-secB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane By similarity.
Cofactor	Binds 1 zinc ion per subunit. Ref.2
Subunit structure	Monomer and homodimer By similarity. Part of the essential Sec protein translocation apparatus which comprises secA, secYEG and auxiliary proteins secDFyajC and yidC/oxaA By similarity.
Subcellular location	Cell inner membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasm By similarity. Note: Distribution is 50-50 By similarity.
Sequence similarities	Belongs to the secA family.

Ontologies

Keywords
Biological process	Protein transport Translocation Transport
Cellular component	Cell inner membrane Cell membrane Cytoplasm Membrane
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	intracellular protein transmembrane transport Inferred from electronic annotation. Source: HAMAP protein import Inferred from electronic annotation. Source: InterPro protein targeting Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell internal side of plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP protein binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 901

901

Protein translocase subunit secA HAMAP MF_01382

PRO_0000109586

Regions

Nucleotide binding

100 – 107

8

ATP Potential

Sites

Metal binding

882

1

Zinc HAMAP MF_01382

Metal binding

884

1

Zinc HAMAP MF_01382

Metal binding

893

1

Zinc HAMAP MF_01382

Metal binding

894

1

Zinc HAMAP MF_01382

Experimental info

Mutagenesis

878

1

R → A: Binds zinc, unable to bind secB. Ref.2

Mutagenesis

879

1

N → A: Binds zinc, unable to bind secB. Ref.2

Mutagenesis

888

1

K → A: Binds zinc, still binds secB. Ref.2

Mutagenesis

889

1

K → A: Binds zinc, unable to bind secB. Ref.2

Mutagenesis

891

1

K → A: Binds zinc, unable to bind secB. Ref.2

Secondary structure

1

.

.

.

.

.

901

Helix Strand Turn

Details...

Beta strand

887 – 889

3

Helix

890 – 892

3

Turn

893 – 895

3

Sequences

	Sequence		Length	Mass (Da)
	P43803-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 2BD0190266BD77AE	FASTA	901	102,587
	10 20 30 40 50 60 MSILTRIFGS RNERVLRKLK KQVVKINKME PAFEALSDDE LKAKTQEFRD RLSGGETLQQ 70 80 90 100 110 120 ILPEAFATVR EASKRVLGMR HFDVQLIGGM VLTNRCIAEM RTGEGKTLTA TLPCYLIALE 130 140 150 160 170 180 GKGVHVVTVN DYLARRDAET NRPLFEFLGM SVGVNIPGLS PEEKRAAYAA DITYATNSEL 190 200 210 220 230 240 GFDYLRDNLA HSKEERFQRT LGYALVDEVD SILIDEARTP LIISGQAENS SELYIAVNKL 250 260 270 280 290 300 IPSLIKQEKE DTEEYQGEGD FTLDLKSKQA HLTERGQEKV EDWLIAQGLM PEGDSLYSPS 310 320 330 340 350 360 RIVLLHHVMA ALRAHTLFEK DVDYIVKDGE IVIVDEHTGR TMAGRRWSDG LHQAIEAKEG 370 380 390 400 410 420 VDVKSENQTV ASISYQNYFR LYERLAGMTG TADTEAFEFQ QIYGLETVVI PTNRPMIRDD 430 440 450 460 470 480 RTDVMFENEQ YKFNAIIEDI KDCVERQQPV LVGTISVEKS EELSKALDKA GIKHNVLNAK 490 500 510 520 530 540 FHQQEAEIVA EAGFPSAVTI ATNMAGRGTD IILGGNWKAQ AAKLENPTQE QIEALKAEWE 550 560 570 580 590 600 KNHEIVMKAG GLHIIGTERH ESRRIDNQLR GRSGRQGDPG SSRFYLSLED GLMRIYLNEG 610 620 630 640 650 660 KLNLMRKAFT VAGEAMESKM LAKVIASAQA KVEAFHFDGR KNLLEYDDVA NDQRHAIYEQ 670 680 690 700 710 720 RNHLLDNDDI SETINAIRHD VFNGVIDQYI PPQSLEEQWD IKGLEERLSQ EFGMELPISN 730 740 750 760 770 780 WLEEDNNLHE ESLRERIVEI AEKEYKEKEA LVGEDAMRHF EKGVMLQTLD ELWKEHLASM 790 800 810 820 830 840 DYLRQGIHLR GYAQKDPKQE YKKESFRMFT EMLDSLKHQV ITALTRVRVR TQEEMEEAER 850 860 870 880 890 900 ARQEMAARIN QNNLPVDENS QTTQNSETED YSDRRIGRNE PCPCGSGKKY KHCHGSRVAR Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[2]	"Structural determinants of SecB recognition by SecA in bacterial protein translocation." Zhou J., Xu Z. Nat. Struct. Biol. 10:942-947(2003) [PubMed: 14517549] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 875-901 IN COMPLEX WITH SECB, MUTAGENESIS OF ARG-878; ASN-879; LYS-888; LYS-889 AND LYS-891, COFACTOR. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L42023 Genomic DNA. Translation: AAC22566.1.

PIR

H64101.

RefSeq

NP_439069.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OZB	X-ray	2.80	I/J	875-901	[»]

ModBase

Search...

Genome annotation databases

GeneID

949911.

GenomeReviews

Gene locus HI0909 in contig L42023_GR.

KEGG

hin:HI0909.

NMPDR

fig|71421.1.peg.875.

TIGR

HI0909.

Phylogenomic databases

HOGENOM

P43803.

OMA

LTGRGVH.

Enzyme and pathway databases

BioCyc

HINF71421:HI_0909-MON.

Family and domain databases

HAMAP

MF_01382.
[Tree]

InterPro

IPR004027. SEC_C_motif.
IPR000185. SecA.
IPR011115. SecA_DEAD.
IPR014018. SecA_motor_DEAD.
IPR011130. SecA_PP_bd.
IPR011116. SecA_Wing/Scaffold.
[Graphical view]

Gene3D

G3DSA:1.10.3060.10. SecA_SW. 1 hit.

Pfam

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.

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_HAEIN

Accession

Primary (citable) accession number: P43803

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 3, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)