SECA_SYNP2
ID SECA_SYNP2 Reviewed; 938 AA.
AC B1XL02;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=SYNPCC7002_A1259;
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT "Complete sequence of Synechococcus sp. PCC 7002.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000951; ACA99257.1; -; Genomic_DNA.
DR RefSeq; WP_012306880.1; NC_010475.1.
DR AlphaFoldDB; B1XL02; -.
DR SMR; B1XL02; -.
DR STRING; 32049.SYNPCC7002_A1259; -.
DR PRIDE; B1XL02; -.
DR EnsemblBacteria; ACA99257; ACA99257; SYNPCC7002_A1259.
DR KEGG; syp:SYNPCC7002_A1259; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_3; -.
DR OMA; MVHYDVQ; -.
DR Proteomes; UP000001688; 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; 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..938
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000145070"
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 938 AA; 107054 MW; D6C677183EC21973 CRC64;
MFKKLFGDPN ARKLKRFQPL VAEINLLAED FANLTDEALA QKTVEFRAKL DKANSDEETE
EILDEILPEA FAVVREAAWR VLQMRHYDVQ LLGGIVLHKG QIAEMRTGEG KTLVATLPAY
LNGLTGKGVH VVTVNDYLAR RDAEWMGQVH RFLGLTVGLI QSSMGPAEKI ENYRCDITYT
TNSELGFDYL RDNMATTIQE VVQRPFNYCI IDEVDSILVD EARTPLIISG QIERPTEKYL
QAAEIAKQLV PQVEEDGPGD YEVDEKARNV LMTDEGFAKA EQLLGVTDLY DEQNPWAHYI
FNAVKAKELF KKDVNYIVRG DEVVIVDEFT GRIMPGRRWS DGLHQAIEAQ EGVTIQKETQ
TLANITYQNF FLLYPKLSGM TGTAKTEETE FEKVYNLEVT IIPTNRPTKR QDLADVVYKN
EKAKWRAVAE ECAQMHETGR PVLVGTTSVE KSEIISAYLH ELGIPHNLLN ARPENVEKES
EIVAQAGRKG AVTIATNMAG RGTDIILGGN SEYMARLKMR EYFMPQIVKP EDEGNFAIAG
SGKNSGGQGF DTNNKQKKKT WKTTLDIYPT ELPTDLEQQL KEAVKFAVDQ YGNQSLTELE
AEEKLAIASE NAPTADPVVQ KLRTVYHAIE KTYHDLTSVE HDEVIQNGGL HVIGTERHES
RRIDNQLRGR AGRQGDPGST RFFLSLEDNL LRIFGGDRVA GLMNAFRVEE DMPIESKMLT
NSLEGAQKKV ETFYYDARKQ VFEYDEVMNN QRRAIYAERR RVLEGQDLKE QVIQYAEKTM
SEIVEAYVNP ELPPEEWKLD KLLDKAKEFI YLLEDLEPKD IEDMTVPEIK TFLHEEVRKA
YDLKEAQVEK SQPGLMRQAE RFFILQQIDT LWREHLQAID ALRESVGLRG YGQKDPLIEY
KQEGYEMFLE MMIDIRRNVV YSLFQFQPQR QPQQPQAV
