HAMAP

Accession	MF_01382
Dates	14-JAN-2008 (Created) 5-DEC-2011 (Last updated, Version 18)

Data class

Protein

Predictors

HAMAP; MF_01382; [distribution of match scores in UniProtKB];[seed alignment for MF_01382]

Names

SecA

Identifier

SECA

Protein name

RecName: Full=Protein translocase subunit SecA;

Gene name

secA

FUNCTION: Has a central role in coupling the hydrolysis of ATP to the transfer of proteins across the thylakoid membrane (By similarity).

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).

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).

FUNCTION: Probably participates in protein translocation into and across both the cytoplasmic and thylakoid membranes in cyanobacterial cells (Potential).

SUBUNIT: Monomer and homodimer (By similarity). Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF-YajC and YidC (By similarity).

SUBUNIT: Monomer and homodimer (By similarity). Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF. Other proteins may also be involved (By similarity).

COFACTOR: May bind 1 zinc ion per subunit (Potential).

SUBCELLULAR LOCATION: Plastid, chloroplast stroma (By similarity). Plastid, chloroplast thylakoid membrane; Peripheral membrane protein (By similarity). Note=A minor fraction is associated with the chloroplast thylakoid membrane (By similarity).

SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side (By similarity). Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Cytoplasm (By similarity).

SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side (By similarity). Cytoplasm (By similarity). Note=Distribution is 50-50 (By similarity).

SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side (By similarity). Cytoplasm (By similarity). Note=Distribution is 50-50 (By similarity).

SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side (By similarity). Cytoplasm (By similarity). Note=Distribution is 50-50 (By similarity).

INDUCTION: Repressed under conditions of excess protein secretion capacity and derepressed when protein secretion becomes limiting. This is regulated by SecM (By similarity).

SIMILARITY: Belongs to the SecA family.

PROSITE	PS01312; SECA; 1; PS51196; SECA_MOTOR_DEAD; 1;
Pfam	PF07517; SecA_DEAD; 1; PF01043; SecA_PP_bind; 1; PF07516; SecA_SW; 1; PF02810; SEC-C; 1;
PRINTS	PR00906; SECA; 1;
TIGRFAMs	TIGR00963; secA; 1;

ATP-binding.

Cytoplasm.

Thylakoid.

Cell membrane, Cell inner membrane.

Cell membrane.

Cell membrane, Cell inner membrane.

Membrane.

Metal-binding, Zinc.

Nucleotide-binding, Protein transport, Translocation, Transport.

GO:0005524; Molecular function: ATP binding.
GO:0065002; Biological process: intracellular protein transmembrane transport.
GO:0006605; Biological process: protein targeting.

GO:0009570; Cellular component: chloroplast stroma.
GO:0009535; Cellular component: chloroplast thylakoid membrane.

GO:0005886; Cellular component: plasma membrane.

GO:0042651; Cellular component: thylakoid membrane.

From: SECA_ECOLI (P10408)
Key		From		To		Description		Condition		FTGroup
NP_BIND		102		109		ATP (Potential)		M-[RKQNDAMFPHGSY]-T-G-E-G-K-[TS]
METAL (Optional)		885		885		Zinc (Potential)		C		1
METAL (Optional)		887		887		Zinc (Potential)		C		1
METAL (Optional)		896		896		Zinc (Potential)		C		1
METAL (Optional)		897		897		Zinc (Potential)		[CH]		1

Size range:	649-1160 amino acids
Related UniRules:	None
Template:	P10408 (SECA_ECOLI); P28366 (SECA_BACSU); P43803 (SECA_HAEIN): [Recover all]
Scope:	Bacteria Plastid
Fusion:	Nter: None; Cter: <Unknown>
Duplicate:	in ALKMQ, BACAH, BACAN, BACCZ, BACHK, BORA1, CHLCH, CLOD6, CORDI, COREF, CORGB, CORGL, CORJK, GEOKA, GEOTN, LACJO, LISIN, LISMF, LISMO, LISW6, MAGSM, MYCBO, MYCBP, MYCLE, MYCPA, MYCS2, MYCSJ, MYCSK, MYCSS, MYCTA, MYCTU, MYCUA, MYCVP, NITHX, NITMU, PEDPA, RHOBA, RHOP5, SILPO, STAA1, STAA3, STAA8, STAAC, STAAE, STAAM, STAAN, STAAR, STAAS, STAAW, STAEQ, STAES, STAHJ, STRA1, STRA3, STRA5, STRAW, STRPN, STRSV, THEFY
Plasmid encoded:	None
Comments:	It is not yet clear whether the form that inserts preproteins into the membrane in conjunction with SecYEG is monmeric or dimeric. In some bacteria that have 2 copies (Listeria, Mycobacteria), 1 copy (secA1) is thought to be essential whereas the other (secA2) is required only for translocation of a subset of proteins. Mycobacteria have 2 copies, with the exception of MYCA1 which only has a copy of secA2. MYCPE has a C- terminal extension that resembles nothing in the database. SECA1_RHOBA (AC Q7UDY6) has a few short inserts compared to other sequences; its length has not been taken into account in the size range. In BAUCH (BCI_0515) it is annotated as a pseudogene with a verfied point mutation leading to a slightly truncated protein. Not encoded in CARRP.