SECA_RHOE4
ID SECA_RHOE4 Reviewed; 947 AA.
AC C0ZWZ6;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=RER_21730;
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC Rhodococcus erythropolis group.
OX NCBI_TaxID=234621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887;
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2005) 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 -!- 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; AP008957; BAH32881.1; -; Genomic_DNA.
DR RefSeq; WP_019747784.1; NC_012490.1.
DR AlphaFoldDB; C0ZWZ6; -.
DR SMR; C0ZWZ6; -.
DR STRING; 234621.RER_21730; -.
DR EnsemblBacteria; BAH32881; BAH32881; RER_21730.
DR GeneID; 57487721; -.
DR KEGG; rer:RER_21730; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_11; -.
DR OMA; MVHYDVQ; -.
DR Proteomes; UP000002204; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR000185; SecA.
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; PS51196; SECA_MOTOR_DEAD; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Cytoplasm; Membrane; Nucleotide-binding;
KW Protein transport; Translocase; Translocation; Transport.
FT CHAIN 1..947
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000215116"
FT REGION 860..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..935
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 105..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 494
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 947 AA; 104781 MW; F103683AE105D34A CRC64;
MPSLSLSKLL RVGEGRMVKR LKHIAEHVES LSPDVEGLTD EQLKAKTTEF RERYAAGETL
DELLPEAFSV AREASWRVID QKHFHVQIMG GAALHFGNVA EMKTGEGKTL TCVLPAYLNA
IAGDGVHVVT VNDYLAKRDS EWMGRVHRAL GLETSVILSG MTPAERRVAY AADITYGTNN
EFGFDYLRDN MTHSLDDLVQ RGHAFAIVDE VDSILIDEAR TPLIISGPAD GSSKWYSEFA
RIAPLLKKDV HYEVDIRKRT IGVHEAGVEL VEDQLGIDNL YEAANSPLVS YLNNAIKAKE
LYTKDKDYIV RDGEVIIVDE FTGRVLVGRR YNEGMHQAIE AKEKVEIKAE NQTLATITLQ
NYFRLYDKLS GMTGTAETEA AELHQTYTLG VIPIPTNRPM VRVDNGDLIY KTEEAKFDAV
VDDVVERHEN GQPVLIGTTS VERSEYLSKQ FTKRGVAHNV LNAKFHEKEA TIIAEAGRSG
AVTVATNMAG RGTDVVLGGN PDIIADIALR KKGLDPVTTP DEYEAAWDAV LDEVKAEVKA
DAEKVRDAGG LYVLGTERHE SRRIDNQLRG RSGRQGDPGE SRFYLSLGDE LMRRFNGSAL
ESIMTRLNLP DDVPIEAKMV SKAIKSAQTQ VEQQNFEIRK NVLKYDEVMN QQRTVIYKER
RQILEGEDME GQVEQMITDV VTAYVDGATA EGYVEDWDLE QLWTALKTLY PVGIDHKTLA
GEDGAGINSD LSRDDLRTAL LEDAHAAYKK REAEIDAIAG ENGMRELERR VFLSVLDRKW
REHLYEMDYL KEGIGLRAMA QRDPLVEYQR EGYDMFIGML DGLKEESVGF LFNLQVEAAP
AQPASGISVT AGSAAAASAT APKPLPTQEA AARTTGTAAP TALRAKGLDD EGPSRLTYTG
PDEDGKAKAT RDSAADSGDG AASRRERREA ARTQSKSNRA PKSKRKR
