SECA1_RHOBA
ID SECA1_RHOBA Reviewed; 1238 AA.
AC Q7UDY6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=RB11690;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01382};
CC Note=May bind 1 zinc ion per subunit. {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 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; BX294153; CAD79269.1; -; Genomic_DNA.
DR RefSeq; NP_870114.1; NC_005027.1.
DR RefSeq; WP_007338547.1; NC_005027.1.
DR AlphaFoldDB; Q7UDY6; -.
DR SMR; Q7UDY6; -.
DR STRING; 243090.RB11690; -.
DR PRIDE; Q7UDY6; -.
DR EnsemblBacteria; CAD79269; CAD79269; RB11690.
DR KEGG; rba:RB11690; -.
DR PATRIC; fig|243090.15.peg.5665; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_1_0_0; -.
DR InParanoid; Q7UDY6; -.
DR OMA; MEWPHLI; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015462; F:ABC-type protein transporter activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 GO; GO:0043952; P:protein transport by the Sec complex; IBA:GO_Central.
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; IPR004027; SEC_C_motif.
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; PF02810; SEC-C; 1.
DR Pfam; PF07517; SecA_DEAD; 1.
DR Pfam; PF01043; SecA_PP_bind; 1.
DR Pfam; PF07516; SecA_SW; 2.
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; 2.
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 Metal-binding; Nucleotide-binding; Protein transport; Reference proteome;
KW Translocase; Translocation; Transport; Zinc.
FT CHAIN 1..1238
FT /note="Protein translocase subunit SecA 1"
FT /id="PRO_0000320919"
FT REGION 1194..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 125..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 570
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 1221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 1223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 1232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 1233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 1238 AA; 139849 MW; 50D2734854D8E4BB CRC64;
MSILERLWDL LGLVFGSTFE RVGSLATSVF GSANARQVAK LQESADRITA MEPKFAAMSD
EELRDQTVLF RKRLREGETL DDIMEEAFAV CREGGKRFLG MRHYDVQLIG GMVLHSGAIG
EMVTGEGKTL VATLPAYLNA LEAKGVHVIT VNDYLARRDM EWMAPLYMNL GLTVDAIQSG
MSTSEKQAAY QCDITYGTNN EFGFDYLRDN MRPAAKGDDR FPSEVQQCQG PLNYAIIDEV
DNILIDEART PLIISGPADL DLGRYGEADR VARQLKKEEH FTVDEKQHNV TLTDEGVRAA
EELAGVESFY TAGNMEWPHL IDNALKAHYL YKLDVNYVVK DKQVVIVDEF TGRLMDGRQW
SDGLHQAVEA KEGVPIKQET QTFATASLQN IFKMYKKLSG MTGTAMTEAD EFWKIYKLDV
VAIPTHRGLQ RIEHPDLIYL TEKDKFKAIA DDVERTHKWD VVVLKDGTEI WGNIKSETDS
VVELLPKGEK QTESFSHEKI VAIERAGRPV LVGTVSIEKS ERLSALLERR GIKHDVLNAK
QHGREADIVS QAGRIGAVTI ATNMAGRGTD IILGGNPETL AWSQLQHKYP TRLEVPDAEW
KALVDEIDER ENMSAEGKIV REIGGLYVLG TERHESRRID LQLRGRCGRQ GDPGGSRFFL
SLEDDLMRIF AGDFVKSMME RMGMKEGEAI ESSLVTRRIA AAQKKVEERN FEIRKSLLEY
DEVMDEQRKR VYRYRQNLLD GHSSREMLLT LIHNEIQSQV ETFLDPNYGV DTFSTFAGGK
LGCQLDARDF QNMDFEMADT YAKDQAERAS EVTVAEAVEE NLPESMEDEW NWKAMATWAN
THLGTNYQDH QLKNKDREEM IDELIAHAHK QIEETDLSEG EPLLEADYGL RVLCAWMRHK
FGIETTPEEF RDVEDRRKVT EELNRRAEAA YTEKEAEYPV LTGISRFTDK QGAQVSLDRE
GLVDWVHGRF NHELSVDEVK LNRDDLKVQL IQYSKQTASA SGGMHAQAAE KVEDLFGRAD
ADVTASLASG QSGKLEALAT WLQEELGNRN TAEDLSRMNR AELTLAVNGA VDDKFHPEMR
RMERQILLNI VDDSWKNHLL TMDHLRSSVG LKGYAQMDPK VEYKREGMRL FESMWDSIGE
RVTDLIFRME SFNDDFIRST WVDARTRHDD AHEAGRSAQQ AAQMESNTAA QRAAAGSEGR
AEGSVDTVRV EEPRIGRNAP CPCGSGKKYK SCCMRRDG
