SECA1_COREF
ID SECA1_COREF Reviewed; 845 AA.
AC Q8FRI7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Protein translocase subunit SecA 1 {ECO:0000255|HAMAP-Rule:MF_01382};
DE EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382};
GN Name=secA1 {ECO:0000255|HAMAP-Rule:MF_01382}; OrderedLocusNames=CE0774;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(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 -!- 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 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}. Note=Distribution is 50-50.
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; BA000035; BAC17584.1; -; Genomic_DNA.
DR RefSeq; WP_011075138.1; NZ_GG700687.1.
DR AlphaFoldDB; Q8FRI7; -.
DR SMR; Q8FRI7; -.
DR STRING; 196164.23492611; -.
DR EnsemblBacteria; BAC17584; BAC17584; BAC17584.
DR KEGG; cef:CE0774; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_2_11; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000001409; 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; 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 membrane; Cytoplasm; Membrane; Nucleotide-binding;
KW Protein transport; Reference proteome; Translocase; Translocation;
KW Transport.
FT CHAIN 1..845
FT /note="Protein translocase subunit SecA 1"
FT /id="PRO_0000318339"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 103..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 845 AA; 95847 MW; E19BB623ECB2C40C CRC64;
MFGLSKMLRV GEGRAVKRLQ KIADQVIALE DQYANLTDEE LKAKTEEFKD RLAQGETLDD
IFLDAFATAR EASWRVLGQK HYKVQIMGGA ALHFGNVAEM RTGEGKTLTC VLPAYLNALE
GKGVHVVTVN DYLAKRDAEW MGRVHRWLGL SVGVILSELR PAERKVAYDC DITYGTNNEL
GFDYLRDNMA RSLNDLVQRG HHYAIVDEVD SILIDEARTP LIISGPVDGS SQWYNVFAQI
VPQLTRDIHY EVDHRKKTVG IKEEGVEKVE DLLGIENLYA PEHSQLVSYL NNAIKAEELF
ERDKDYIVRN GEVMIVDGFT GRVLAGRRYN EGMHQAIEAK EKVEIKNENQ TLATVTLQNY
FRLYEKLSGM TGTAETEAAE LHQIYKLDVI QIPTNRENQR DDLTDLVYKT QEAKFAAVVD
DIAERIANGQ PVLVGTVSVE RSEYLSQLLT RRGIKHNVLN AKHHEQEAQI VAQAGLPGAV
TVATNMAGRG TDIVLGGNPD ILLDIKLRER GLDPFEDEEA YQVAWEEELP KMKQRCEERA
EKVREAGGLY VLGTERHESR RIDNQLRGRA GRQGDPGATR FYLSMRDDLM VRFVGPTMEN
MMNRLNVPDD VPIESKTVTN SIKGAQAQVE NQNFEMRKNV LKYDEVMNEQ RKVIYSERRE
ILESSDISHY IKNMVDETIS AYVAAATANG YVEDWDLDKL WNALEALYGP TFTWQSLVDG
SEYGAPGELS AEDLRTALLE DARAEYAKLE EAVTALGGEA QMRNIERMVL MPVIDQKWRE
HLYEMDYLKE GIGLRAMAQR DPLVEYQKEG GDMFNAMKEA IKEETVRQLF LMRKQFVKQD
EEANA
