ID SECA_GLOC7 Reviewed; 935 AA.
AC B7K818;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Protein translocase subunit SecA {ECO:0000255|HAMAP-Rule:MF_01382};
DE EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382};
GN Name=secA {ECO:0000255|HAMAP-Rule:MF_01382};
GN OrderedLocusNames=PCC7424_0032;
OS Gloeothece citriformis (strain PCC 7424) (Cyanothece sp. (strain PCC
OS 7424)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Gloeothece; Gloeothece citriformis.
OX NCBI_TaxID=65393;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7424;
RX PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA Sherman L.A., Pakrasi H.B.;
RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT unicellular nitrogen-fixing Cyanobacteria.";
RL MBio 2:E214-E214(2011).
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. {ECO:0000255|HAMAP-Rule:MF_01382}.
CC -!- FUNCTION: Probably participates in protein translocation into and
CC across both the cytoplasmic and thylakoid membranes in cyanobacterial
CC cells. {ECO:0000255|HAMAP-Rule:MF_01382}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate +
CC cellular proteinSide 2.; EC=7.4.2.8; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01382};
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.
CC {ECO:0000255|HAMAP-Rule:MF_01382}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01382}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01382}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}.
CC Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01382};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01382};
CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}. Cytoplasm
CC {ECO:0000255|HAMAP-Rule:MF_01382}.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
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DR EMBL; CP001291; ACK68506.1; -; Genomic_DNA.
DR RefSeq; WP_012597457.1; NC_011729.1.
DR AlphaFoldDB; B7K818; -.
DR SMR; B7K818; -.
DR STRING; 65393.PCC7424_0032; -.
DR KEGG; cyc:PCC7424_0032; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_3; -.
DR OrthoDB; 9805579at2; -.
DR Proteomes; UP000002384; Chromosome.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008564; F:protein-exporting ATPase activity; IEA:UniProtKB-EC.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR GO; GO:0017038; P:protein import; IEA:InterPro.
DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule.
DR CDD; cd17928; DEXDc_SecA; 1.
DR CDD; cd18803; SF2_C_secA; 1.
DR Gene3D; 1.10.3060.10; Helical scaffold and wing domains of SecA; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.90.1440.10; SecA, preprotein cross-linking domain; 1.
DR HAMAP; MF_01382; SecA; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000185; SecA.
DR InterPro; IPR020937; SecA_CS.
DR InterPro; IPR011115; SecA_DEAD.
DR InterPro; IPR014018; SecA_motor_DEAD.
DR InterPro; IPR011130; SecA_preprotein_X-link_dom.
DR InterPro; IPR044722; SecA_SF2_C.
DR InterPro; IPR011116; SecA_Wing/Scaffold.
DR InterPro; IPR036266; SecA_Wing/Scaffold_sf.
DR InterPro; IPR036670; SecA_X-link_sf.
DR NCBIfam; TIGR00963; secA; 1.
DR PANTHER; PTHR30612:SF0; CHLOROPLAST PROTEIN-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR30612; SECA INNER MEMBRANE COMPONENT OF SEC PROTEIN SECRETION SYSTEM; 1.
DR Pfam; PF21090; P-loop_SecA; 1.
DR Pfam; PF07517; SecA_DEAD; 1.
DR Pfam; PF01043; SecA_PP_bind; 1.
DR Pfam; PF07516; SecA_SW; 1.
DR PRINTS; PR00906; SECA.
DR SMART; SM00957; SecA_DEAD; 1.
DR SMART; SM00958; SecA_PP_bind; 1.
DR SUPFAM; SSF81886; Helical scaffold and wing domains of SecA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF81767; Pre-protein crosslinking domain of SecA; 1.
DR PROSITE; PS01312; SECA; 1.
DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Cytoplasm; Membrane;
KW Nucleotide-binding; Protein transport; Reference proteome; Thylakoid;
KW Translocase; Translocation; Transport.
FT CHAIN 1..935
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000144999"
FT BINDING 90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 108..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 504
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 935 AA; 106990 MW; FC9766C034ED2897 CRC64;
MLKALFGDPN TRKLNKFQSL VTETNLLEEE IKKLSDEELK RKTDEFREEL EKASNDRELE
EILDEILPEA FALVREASLR VLGMRHFDVQ LMGGIVLHKG QIAEMKTGEG KTLVSTLPAY
LNGLTGKGVH IVTVNDYLAR RDAEWMGQVH RFLGLSVGLI QSGMSPEDRK KNYACDITYT
TNSELGFDYL RDNMATSMAE VVQRPFNFCV IDEVDSILID EARTPLIISG PIDRPTEKYI
QASQIAKQLV KQEVEDGPGD YEVDEKARNI LLTDEGYKKA EQLLGVKDLF DQDNPWAHYI
FNAIKAKELF TKDVNYIVRG GEVVIVDEFT GRVLAGRRWS DGLHQAIEAK ERVEIQQETQ
TLATITYQNF FLLYPKLSGM TGTAKTEETE LEKVYNLQVT IIPTNRPSQR YDLPDAVYKA
ERGKWMAVAE EVEELHQKGR PILVGTTSVE KSELLSNLLR QKEIPHNLLN ARPENVERES
EIVAQAGRKG AVTIATNMAG RGTDIILGGN SDYMSRLKIR EYLMPKLVKP EEDELAVNVP
SLGGKRSRPQ GFASDKKVKT WKASPDIFPT ELSEETVKAL KEAVKIAVDQ HGQQSLGELE
AEEKIAIASE NAPTDDIVIQ KLREVYKKIR AEYEIFTSKE HNEVVELGGL HVMGTERHES
RRIDNQLRGR AGRQGDPGST RFFLSLEDNL LKIFGGDRVA RLMDALQVEE DMPIESGMLT
RSLEGAQKKV ETYYYDIRKQ VFEYDEVMNN QRKAIYAERR RVLEGLDLKE QVLQYAEKTM
DEIVEAYVNP DLPPEEWDLN TLVSKVKEFV YLLQDVAPSD IEDMTFMEMK NFLHEEVRKA
YEVKEQEVDR VRPGLMRDAE RFFILQQIDT LWREHLQGME SLRESIGLRG YGQKDPLIEY
KQEGYEMFLE MMIDIRRNVV YSLFQFKPQG QPQAV
//
