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SECA_GLOC7
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   03-AUG-2022, entry version 73.
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; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   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   PRIDE; B7K818; -.
DR   EnsemblBacteria; ACK68506; ACK68506; PCC7424_0032.
DR   KEGG; cyc:PCC7424_0032; -.
DR   eggNOG; COG0653; Bacteria.
DR   HOGENOM; CLU_005314_3_0_3; -.
DR   OMA; MVHYDVQ; -.
DR   OrthoDB; 212453at2; -.
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; cd18803; SF2_C_secA; 1.
DR   Gene3D; 3.40.50.300; -; 2.
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   PANTHER; PTHR30612; PTHR30612; 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; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF81767; SSF81767; 1.
DR   SUPFAM; SSF81886; SSF81886; 1.
DR   TIGRFAMs; TIGR00963; 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
 
 
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