SECA3_MAGMM
ID SECA3_MAGMM Reviewed; 658 AA.
AC A0L9N3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Protein translocase subunit SecA 3 {ECO:0000255|HAMAP-Rule:MF_01382};
DE EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382};
GN Name=secA3 {ECO:0000255|HAMAP-Rule:MF_01382}; OrderedLocusNames=Mmc1_2175;
OS Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales;
OC Magnetococcaceae; Magnetococcus.
OX NCBI_TaxID=156889;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX PubMed=19465526; DOI=10.1128/aem.02874-08;
RA Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT coccus strain MC-1.";
RL Appl. Environ. Microbiol. 75:4835-4852(2009).
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 both as a receptor for the
CC preprotein-SecB complex and as an ATP-driven molecular motor driving
CC the stepwise translocation of polypeptide chains across the membrane.
CC {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-YajC and YidC. {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 Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50-
CC 50. {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; CP000471; ABK44676.1; -; Genomic_DNA.
DR RefSeq; WP_011713804.1; NC_008576.1.
DR AlphaFoldDB; A0L9N3; -.
DR SMR; A0L9N3; -.
DR STRING; 156889.Mmc1_2175; -.
DR EnsemblBacteria; ABK44676; ABK44676; Mmc1_2175.
DR KEGG; mgm:Mmc1_2175; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_2_5; -.
DR OMA; WADHLAF; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000002586; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma 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; IPR036670; SecA_X-link_sf.
DR PANTHER; PTHR30612; PTHR30612; 1.
DR Pfam; PF07517; SecA_DEAD; 1.
DR Pfam; PF01043; SecA_PP_bind; 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 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; Translocase;
KW Translocation; Transport.
FT CHAIN 1..658
FT /note="Protein translocase subunit SecA 3"
FT /id="PRO_0000318373"
FT BINDING 111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 129..133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 536
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 658 AA; 73776 MW; 3FF025DE1013E02F CRC64;
MFNLSLHGDP YPQQPGHLQL SWLDRMGERV RLAWMRHKQV NGWVLGRMAK RVLKAQTERE
SMTPEALRED LQRLTLALRR DGLEDALVEQ AFAHVRLTAQ RVLGMAHFPV QLKGGYIMLM
GYLAEMDTGE GKTLTATLPA ATAALAGFTV HVVTVNEYLA RRDAQLMTPL YRALGVTTGV
VTESMDSDEK QLGYRANVVY CTSKTLVFDY LRDRIQLGER MKPMAMAFDA LVGGGRGQVM
LQGLQYAIVD EADSIFVDEA RTPLIISAPS KDASELAFLH TAWSLSQQLQ QGQDYTLSGE
EPPRITEAGS AQLAQLCVDL PPVWQGQHRR EEAVAQALTA QHSFDRDVHY IIRDDKVMVV
DETTGRVMPD RAWERGLQQL IEIKEGVAVT PPKETLAKIS FQLFFRRFLR LSGMSGTCRE
VGGEIAEVYG LGVVRVAPNR PSKRKNLPIA LYAWRAQADA AVVQAVRRCH MLGQPVLVGT
RSIAASELLS QSFSEAGLPH RVLNAKQDQE ENTIIAEAGY KGGITIATNM AGRGTDIKLS
KEVQACGGLH VILTERHDNR RVDRQLAGRC ARQGDPGSWQ EILSLEDELT QKFLPLLGRT
LRAWLALMPH FFLARWLGMV YYRWAQSYAD RGHRRVRRQL MKTDFQLRQS LSFTGEME
