SECA_RENSM
ID SECA_RENSM Reviewed; 932 AA.
AC A9WMN9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
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};
GN OrderedLocusNames=RSal33209_1631;
OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS NBRC 15589 / NCIMB 2235).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Renibacterium.
OX NCBI_TaxID=288705;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235;
RX PubMed=18723615; DOI=10.1128/jb.00721-08;
RA Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT reductive evolution away from an environmental Arthrobacter ancestor.";
RL J. Bacteriol. 190:6970-6982(2008).
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; CP000910; ABY23367.1; -; Genomic_DNA.
DR RefSeq; WP_012245042.1; NC_010168.1.
DR AlphaFoldDB; A9WMN9; -.
DR SMR; A9WMN9; -.
DR STRING; 288705.RSal33209_1631; -.
DR EnsemblBacteria; ABY23367; ABY23367; RSal33209_1631.
DR KEGG; rsa:RSal33209_1631; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_11; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000002007; 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..932
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000087327"
FT REGION 857..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 104..108
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 932 AA; 103371 MW; E57601CF899BADF8 CRC64;
MPSLFEKILR TGDRKTLKRL HVYADAINTL EDSFQTFTDA ELREETDKLR ARHADGESLD
DLLPEAFAAV REGSRRTLGM RQFDVQLMGG AALHLGNIAE MKTGEGKTLV ATAPAYLNGL
SGKGVHIVTT NDYLASYQSE LMGRVHRFMG LTSGCILSAQ EPSERRLQYA ADVTYGTNNE
FGFDYLRDNM AWSSEELVQR GHHFAIVDEV DSILIDEART PLIISGPASG DANRWYGEFA
KVVLRLDVDD DYEVDEKKRT VGVLEPGIEK VEDYLGISNL YESANTPLIG FLNNAIKAKE
LFKRDKDYVI LDGEVLIVDE HTGRILAGRR YNEGMHQAIE AKESVEIKAE NQTLATVTLQ
NYFRLYEKLS GMTGTAETEA SEFMGTYELG VVAIPTNKPM VRIDQSDLVY KNEVVKFEAV
VKDIEERHKE GQPVLVGTTS VEKSEYLSKQ LSKLGIKHEV LNAKNHAREA SIVAQAGRKG
AVTVATNMAG RGTDIMLGGN AEFNAVTELA KRGLDPEETP EEYEAAWAEA YEKAQEATEE
EHEEVVELGG LYVLGTERHE SRRIDNQLRG RSGRQGDPGE SRFYLSLTDD LMRLFNSGAA
ERLMGRSVMP DDQALESKLV SKAIASAQGQ VEGRNAEQRK NVLKYDDVLN RQREAIYGDR
RRILEGDDLH EKVQHFLEDT VNESIDATTA EGHAEGWDYK ALWSSLGTLY PIGLTADDVA
EEVGGLANVT SDVLKREILS DAKLAYQGRE EKLGSETIRE LERRVVLSVI GRKWQEHLYE
MDYLKEGIGL RAMAQRDPLV EYQREGFVMF QAMMGAIREE SVGFLFNLEV QVEEAPAASA
GVQANQPSAL LDRVNGEDAG AEAHASAKPV LNAPGLAEPE RPSQLQFTAP DASGEAETRI
ERRSTAGSAG DSNLPPSARK TNKPAPKRKK RR
