SECA_PARD8
ID SECA_PARD8 Reviewed; 1126 AA.
AC A6L997;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=BDI_0484;
OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS 5825 / NCTC 11152).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=435591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(2007).
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; CP000140; ABR42261.1; -; Genomic_DNA.
DR RefSeq; WP_005855607.1; NZ_LR215978.1.
DR AlphaFoldDB; A6L997; -.
DR SMR; A6L997; -.
DR STRING; 435591.BDI_0484; -.
DR EnsemblBacteria; ABR42261; ABR42261; BDI_0484.
DR GeneID; 57234553; -.
DR KEGG; pdi:BDI_0484; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_10; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR BioCyc; PDIS435591:G1G5A-499-MON; -.
DR Proteomes; UP000000566; 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: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 CDD; cd18803; SF2_C_secA; 1.
DR Gene3D; 3.40.50.300; -; 3.
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; 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; 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 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..1126
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000320880"
FT REGION 1060..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1077
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1092
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 193..197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 694
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 1110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 1112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 1121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 1122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 1126 AA; 128964 MW; A88BADC5CB527D91 CRC64;
MGFNEFMTKL FGNKSQRDLK EITPYVDKVK AVYPSIKALS NDELRAKTDE IKQRIQDYVA
EEKAQVEELR KGIEDKELEE REAIWAEVDK IEKAITDKME VVLEQSLPEV FAIMKDTARR
FAENEEVVVT ANQFDRDLAA RFDFVRIEDD KAIYANHWKA GGNEITWDMI HYDVQLFGGV
VLHKGKIAEM ATGEGKTLVA TLPVFLNALT RNGVHVVTVN DYLSKRDSEW MGPLYMFHGL
SVDCIDKHQP NSEARRKAYE ADITFGTNNE FGFDYLRDNM AISPKDLVQR KHNYSIVDEV
DSVLIDDART PLIISGPIPR GEEQLFEQFR PNVEVVVNAQ KDLCSKLLIE AKKKMASDDQ
KVVEEGSILL YRSFKGYPRN KALIKFLSEQ GVKAQMLKTE EYFMSENMRH MHEATDELYF
VIDEKNNSIE LTDKGIDLLT GKTDDPTFFV LPDITSQLSQ LENMTGTEEE KQAQKDEILA
NYSVKSERVH TINQLLKAYT LFEKDDEYVV MDNKVMIVDE QTGRIMDGRR YSDGLHQAIE
AKERVKVEAA TQTFATITLQ NYFRMYHKLS GMTGTAETEA GEFWDIYKLD VVVIPTNRPI
ARNDMNDRIY KTKREKYNAV IEEIVQLTEA GRPVLVGTTS VEISELLSRM LTMRKIQHNV
LNAKLHQKEA EIVALAGQKS TVTIATNMAG RGTDIKLSKD VKDAGGLAII GTERHESRRV
DRQLRGRAGR QGDPGSSVFF VSLEDDLMRL FASEKIAGLM DKLGFKEGEV LEHNMLSKSV
ERAQKKVEEN NFGIRKRLLE YDDVMNSQRN VIYTRRRHAL MGERIGLDVL NTIYDTSTAI
ADQHAEDFEG FKLELFKTFA MESPFTEDEF KSMKPEQLVE KLFEEALKTY KRRMERMTQV
AHPVIKQVYE NQGAMYENIM IPITDGKRMY NVSCNLKEAY DTECKAIVKS FQKSIVLHMI
DEGWKEHLRE MDELRHSVQN ASYENKDPLL IYKLESYNLF KTMVDNMNRK TAAILMRGQI
PVREEPTEEQ RQAMQARQAA VAQQAAQAIA EERARQRIAV QEAAPEKHED MSRYRTEKTD
LSGNNTQAEA PQPKQAPVRA EKRVGRNDPC PCGSGKKYKN CHGQGL
