SECA_KORVE
ID SECA_KORVE Reviewed; 993 AA.
AC Q1IMP4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=Acid345_2855;
OS Koribacter versatilis (strain Ellin345).
OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae;
OC Candidatus Koribacter.
OX NCBI_TaxID=204669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin345;
RX PubMed=19201974; DOI=10.1128/aem.02294-08;
RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT "Three genomes from the phylum Acidobacteria provide insight into the
RT lifestyles of these microorganisms in soils.";
RL Appl. Environ. Microbiol. 75:2046-2056(2009).
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; CP000360; ABF41856.1; -; Genomic_DNA.
DR RefSeq; WP_011523657.1; NC_008009.1.
DR AlphaFoldDB; Q1IMP4; -.
DR SMR; Q1IMP4; -.
DR STRING; 204669.Acid345_2855; -.
DR PRIDE; Q1IMP4; -.
DR EnsemblBacteria; ABF41856; ABF41856; Acid345_2855.
DR KEGG; aba:Acid345_2855; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_0; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000002432; 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; -; 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; 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 inner membrane; Cell membrane; Cytoplasm; Membrane;
KW Metal-binding; Nucleotide-binding; Protein transport; Reference proteome;
KW Translocase; Translocation; Transport; Zinc.
FT CHAIN 1..993
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000318302"
FT REGION 910..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..952
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 120..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 523
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 979
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 981
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 990
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 991
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 993 AA; 113311 MW; 1193BEA5A31FA3FB CRC64;
MINKAIAKIF GTQNEREIKR LMPIVAQINA LEPQVKQFSD DQLRAKTDEF RAKIQERLAK
YEEAEHKNHA LKEVLDEILP EAFAICREAG WRVLNMRHFD VQLIGGMVLH SGRISEMKTG
EGKTLVATLP VYLNALSGRG VHVVTVNDYL AKRDSEWMGK LYNFLGLSVG VIVHDLDDDQ
RREAYRADVT YGTNNEFGFD YLRDNMKFEL SDCVQREFNF AIVDEVDSIL IDEARTPLII
SGASEESTDK YQRVNVIIPR LEKGEEIEGR EPGDKILTGD YVVDEKHKTI TVSDDGWEKV
EKLLGIGNIA DPENWDLKHH VEVAIKAHAL YHVDVEYVVK DGEVLIVDEF TGRLMPGRRW
SDGLHQAVEA KEGVKVEREN QTLATITFQN YFRLYKKLAG MTGTAETEAA EFDKIYKLEV
VVIPTNRTLL RKENPDVVYR TEKEKFFAVA DEIAKLSVSQ QPVLVGTVSI EKSERLSELL
KRKNIKHVVL NAKFHEREAE YVAQAGRLGQ VTIATNMAGR GTDILLGGNP EFMAKQETLK
KGVAQPVHAA GGEVDARPDD PNTVYWYYAG NEYVCPRAQW EEILAHYKTQ TDFEHEQVKQ
AGGLFILGTE RHESRRIDNQ LRGRAGRQGD PGASRFYLSL EDDLMRIFAK EWVSTLLQRL
GMEEGVPIES KMISRRIEKA QEAVEAQNFE ARKHLLEYDD VMNKQRMAVY GLRRQLLEGL
DQKELIIDEY VTEILGDLLD KFAPTEKHPE DWDIAGLKGE IFTRFGVDII AEGVEPEKLN
RMQLGDGIFD KLKERYEAKE QLIGNDQMRH HERVIMLSVI DQLWKDHLLN MDHLKEGIGL
RGYAQHDPLV EYKRESFDMF EGMMATFKEQ TVRYLYLMQI IDAATNMPVE IPRRRAPENV
RELGPVLEAE NAPEPQISGG NGQQPPQRRQ QTSLDDLEKQ FERKKKRELE QARMAGGGMP
DAVQQVVRSG DKIGRNDPCF CGSGKKYKKC HGA
