SECA_MICAN
ID SECA_MICAN Reviewed; 938 AA.
AC B0JLJ4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 92.
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}; OrderedLocusNames=MAE_31960;
OS Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Microcystaceae; Microcystis.
OX NCBI_TaxID=449447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-843 / IAM M-247;
RX PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT Microcystis aeruginosa NIES-843.";
RL DNA Res. 14:247-256(2007).
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; AP009552; BAG03018.1; -; Genomic_DNA.
DR RefSeq; WP_012266145.1; NC_010296.1.
DR AlphaFoldDB; B0JLJ4; -.
DR SMR; B0JLJ4; -.
DR STRING; 449447.MAE_31960; -.
DR PaxDb; B0JLJ4; -.
DR EnsemblBacteria; BAG03018; BAG03018; MAE_31960.
DR KEGG; mar:MAE_31960; -.
DR PATRIC; fig|449447.4.peg.2897; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_3; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR BioCyc; MAER449447:MAE_RS13850-MON; -.
DR Proteomes; UP000001510; 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_1000145034"
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; 107146 MW; 06E10F122CE9C96A CRC64;
MLKALLGDPN ARKIKKFQPL VTEINLLEED IKNLSDEELR SKTSEFKERL DKARNYDERE
EILEEILPEA FAIVREAGIR VLGMRHFDVQ LLGGMVLHKG QIAEMKTGEG KTLVATLPAY
LNGLTGKGVH VVTVNDYLAR RDAEWMGQVH RFLGLSVGLI QAGMSPEERK KNYACDITYT
TNSELGFDYL RDNMATVMGE VVQRPFNYCV IDEVDSILID EARTPLIISG PIDRPTEKYI
LAAEIAKQLV RQKVEDGPGD YEVNEKDRNV LMTDEGFKRA EELLGVTDLY DQENPWAHYI
SNAIRAKELQ KKDVNYIVRS GEIVIVDEFT GRVLPGRRWG DGLHQAVEAK EGVEIQQETQ
TLATITYQNF FLLYPKLSGM TGTAKTEETE LEKVYNLQVT IIPTNRVSRR QDLADVVYKN
EQAKWNAVAE ECQQMHEQGR PVLVGTTSVE KSEVLSLLLQ GRNIPHNLLN ARPENVERES
EIVAQAGRAG AVTIATNMAG RGTDIILGGN SDYMARLKIR EYLMPKLVMP EDDNLAFSLP
SLGERNRPQG FAPGKKKKNW RASAEIFPTE LPKEVENALK EAVKFAVDTH GTQSLPELEV
EEKIAIAAEK APTDDPVIQK LREVYKLIRK SYEDYTGKEH DEVVERGGLH VIGTERHESR
RIDNQLRGRA GRQGDPGSTH FFLSLEDNLL RIFGGDRVAG LMDAFRVEED MPIESGMLTR
SLEGAQRKVE TFYYDARKQV FEYDEVMNNQ RRAIYAERRR VLEGMDLKEQ VLQYAEKTMD
EIVMAYVNPE LPAEEWDLEK LISKSQEFVY LLADITAKDV EEMSVNDIKM FLHEEVRKAY
EIKERQVDSI RAGLMRDAER YFILQQIDML WREHLQAMEA LRESIGLRGY GQKDPLIEYK
QEGYEMFLEM MIDIRRNVVY SLFQFQPQGQ PQAVASEQ
