SECA_PARMW
ID SECA_PARMW Reviewed; 937 AA.
AC Q7UA15;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=SYNW0086;
OS Parasynechococcus marenigrum (strain WH8102).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Parasynechococcus; Parasynechococcus marenigrum.
OX NCBI_TaxID=84588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH8102;
RX PubMed=12917641; DOI=10.1038/nature01943;
RA Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT "The genome of a motile marine Synechococcus.";
RL Nature 424:1037-1042(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX569689; CAE06601.1; -; Genomic_DNA.
DR RefSeq; WP_011126964.1; NC_005070.1.
DR AlphaFoldDB; Q7UA15; -.
DR SMR; Q7UA15; -.
DR STRING; 84588.SYNW0086; -.
DR PRIDE; Q7UA15; -.
DR EnsemblBacteria; CAE06601; CAE06601; SYNW0086.
DR KEGG; syw:SYNW0086; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_3; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000001422; 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; Thylakoid; Translocase;
KW Translocation; Transport.
FT CHAIN 1..937
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000318475"
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 509
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 937 AA; 105841 MW; BD85AABF9FF69898 CRC64;
MLKLLLGDPN ARKLKRYQPI VSDINLLEED IFPLSDDALR DKTAAFQEQL ASAGSLENQR
PILDEILPEA FAVVREAGKR VLGMRHFDVQ LIGGMVLHEG QIAEMKTGEG KTLVATLPSY
LNALTGRGVH VVTVNDYLAR RDAEWMGQVH RFLGLSVGLI QQDMRPEERR RNYNCDITYA
TNSELGFDYL RDNMAADISE VVQREFQYCV IDEVDSILID EARTPLIISG QVQRPQEKYQ
QAAQVAQALT RAAEMGKDGI DPEGDYEVDE KQRSCTLTDE GFAKAEQMLG VQDLFDPQDP
WAHYITNALK AKDLFVKDVN YIVRDGEAVI VDEFTGRVMP GRRWSDGQHQ AIEAKEALPI
QAETQTLASI TYQNFFLLYP RLAGMTGTAK TEEVEFEKTY KLETTIVPTN RVRARQDWPD
QVYKTETAKW RAVANETVDI HKNGRPVLVG TTSVEKSELL SALLAEQEIP HNLLNAKPEN
VERESEIVAQ AGRAGAVTIA TNMAGRGTDI ILGGNSDYMA RLKLREVLLG RLVKPEENHK
PPVPLQRNAA AGFSEAPTAS ATPSRDSLYP CVLTDDTDQT LAQLARDLVK AWGDRALTLI
ELEERIATAA EKAPTDDPNI QALRAATARV KGEFDAVVKQ EEQRVREAGG LHVIGTERHE
SRRVDNQLRG RAGRQGDPGS TRFFLSLGDN LLRIFGGDRV AGLMNAFRVE EDMPIESGML
TRSLEGAQKK VETYYYDIRK QVFEYDEVMN NQRRAVYSER RRVLDGRALK KQVIGYGERT
MNEIVEAYVN PDLPPEEWDT AQLVAKVKEF VYLLEDLTPE QVQGLGMDEL KAFLQEQLRN
AYDIKEGQVE QQRPGLMREA ERFFILQQID TLWREHLQAM DALRESVGLR GYGQKDPLIE
YKNEGYDMFL EMMTNMRRNV IYSMFMFQPA APQQSQV
