AC MF_01382; DC Protein; auto TR HAMAP; MF_01382; -; 1; level=0 XX Names: SecA XX ID SECA DE RecName: Full=Protein translocase subunit SecA; DE EC=7.4.2.8; GN Name=secA; XX case CC -!- FUNCTION: Has a central role in coupling the hydrolysis of ATP to the CC transfer of proteins across the thylakoid membrane. else case or or CC -!- FUNCTION: Part of the Sec protein translocase complex. Interacts with CC the SecYEG preprotein conducting channel. Has a central role in CC coupling the hydrolysis of ATP to the transfer of proteins into and CC across the cell membrane, serving both as a receptor for the CC preprotein-SecB complex and as an ATP-driven molecular motor driving CC the stepwise translocation of polypeptide chains across the membrane. else CC -!- FUNCTION: Part of the Sec protein translocase complex. Interacts with CC the SecYEG preprotein conducting channel. Has a central role in CC coupling the hydrolysis of ATP to the transfer of proteins into and CC across the cell membrane, serving as an ATP-driven molecular motor CC driving the stepwise translocation of polypeptide chains across the CC membrane. end case case and not CC -!- FUNCTION: Probably participates in protein translocation into and CC across both the cytoplasmic and thylakoid membranes in cyanobacterial CC cells. end case CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate + CC cellular proteinSide 2.; EC=7.4.2.8; case CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=May bind 1 zinc ion per subunit.; end case case CC -!- SUBUNIT: Monomer and homodimer. Part of the essential Sec protein CC translocation apparatus which comprises SecA, SecYEG and auxiliary CC proteins SecDF-YajC and YidC. else case not CC -!- SUBUNIT: Monomer and homodimer. Part of the essential Sec protein CC translocation apparatus which comprises SecA, SecYEG and auxiliary CC proteins SecDF. Other proteins may also be involved. end case case CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Plastid, chloroplast CC thylakoid membrane; Peripheral membrane protein. Note=A minor fraction CC is associated with the chloroplast thylakoid membrane. else case and not CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; CC Cytoplasmic side. Cellular thylakoid membrane; Peripheral membrane CC protein; Cytoplasmic side. Cytoplasm. else case CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; CC Cytoplasmic side. Cytoplasm. Note=Distribution is 50-50. else case not defined or CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; CC Cytoplasmic side. Cytoplasm. Note=Distribution is 50-50. else case CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; CC Cytoplasmic side. Cytoplasm. Note=Distribution is 50-50. end case case CC -!- INDUCTION: Repressed under conditions of excess protein secretion CC capacity and derepressed when protein secretion becomes limiting. This CC is regulated by SecM. end case CC -!- SIMILARITY: Belongs to the SecA family. XX DR PROSITE; PS01312; SECA; 1; trigger=no DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1; trigger=no DR Pfam; PF07517; SecA_DEAD; 1; trigger=no DR Pfam; PF01043; SecA_PP_bind; 1; trigger=no DR Pfam; PF07516; SecA_SW; 1; trigger=no DR Pfam; PF02810; SEC-C; 1; trigger=no DR PRINTS; PR00906; SECA; 1; trigger=no DR NCBIfam; TIGR00963; SecA; 1; trigger=no XX KW ATP-binding case not KW Cytoplasm end case case or and not KW Thylakoid else case KW Cell membrane KW Cell inner membrane else case not defined or KW Cell membrane else case KW Cell membrane KW Cell inner membrane end case KW Membrane case KW Metal-binding KW Zinc end case KW Nucleotide-binding KW Protein transport KW Translocase KW Translocation KW Transport XX GO GO:0005524; F:ATP binding GO GO:0065002; P:intracellular protein transmembrane transport GO GO:0006605; P:protein targeting case GO GO:0009570; C:chloroplast stroma GO GO:0009535; C:chloroplast thylakoid membrane else GO GO:0005886; C:plasma membrane end case case and not GO GO:0042651; C:thylakoid membrane end case XX FT From: SECA_BACSU (P28366) FT BINDING 103..107 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: G-E-G-K-[TS] FT BINDING 825 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Optional; Group: 1; Condition: C FT BINDING 827 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Optional; Group: 1; Condition: C FT BINDING 836 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Optional; Group: 1; Condition: C FT BINDING 837 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Optional; Group: 1; Condition: [CH] FT BINDING 85 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: Q FT BINDING 492 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: D XX Size: 649-1160; Related: None; Template: P10408; P28366; P43803; Scope: Bacteria Plastid Fusion: Nter: None Cter: Duplicate: in ALKMQ, BACAH, BACAN, BACCZ, BACHK, BORA1, CHLCH, CLOD6, CORDI, COREF, CORGB, CORGL, CORJK, GEOKA, GEOTN, LACJO, LISIN, LISMF, LISMO, LISW6, MAGMM, MYCBO, MYCBP, MYCLE, MYCPA, MYCS2, MYCSJ, MYCSK, MYCSS, MYCTA, MYCTU, MYCUA, MYCVP, NITHX, NITMU, PEDPA, RHOBA, RHOP5, RUEPO, STAA1, STAA3, STAA8, STAAC, STAAE, STAAM, STAAN, STAAR, STAAS, STAAW, STAEQ, STAES, STAHJ, STRA1, STRA3, STRA5, STRAW, STRPN, STRSV, THEFY Plasmid: 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. MALP2 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. XX # Revision 1.36 2023/06/01 //