SECA_ZYMMO
ID SECA_ZYMMO Reviewed; 925 AA.
AC Q5NP12;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 108.
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=ZMO0924;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
RN [2]
RP SEQUENCE REVISION TO 104.
RX PubMed=19816441; DOI=10.1038/nbt1009-893;
RA Yang S., Pappas K.M., Hauser L.J., Land M.L., Chen G.L., Hurst G.B.,
RA Pan C., Kouvelis V.N., Typas M.A., Pelletier D.A., Klingeman D.M.,
RA Chang Y.J., Samatova N.F., Brown S.D.;
RT "Improved genome annotation for Zymomonas mobilis.";
RL Nat. Biotechnol. 27:893-894(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 both as a receptor for the
CC preprotein-SecB complex and as an ATP-driven molecular motor driving
CC the stepwise translocation of polypeptide chains across the membrane.
CC {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-YajC and YidC. {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; AE008692; AAV89548.2; -; Genomic_DNA.
DR RefSeq; WP_011240783.1; NZ_CP035711.1.
DR AlphaFoldDB; Q5NP12; -.
DR SMR; Q5NP12; -.
DR STRING; 264203.ZMO0924; -.
DR PRIDE; Q5NP12; -.
DR EnsemblBacteria; AAV89548; AAV89548; ZMO0924.
DR GeneID; 58026723; -.
DR KEGG; zmo:ZMO0924; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_5; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000001173; 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; 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 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..925
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000321057"
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 499
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 906
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 908
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 917
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 918
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 925 AA; 104978 MW; 9119142A8740878C CRC64;
MFGAIAKALF GSANDRYIKS LRRIVEKVNS FEPSVSALDD DGLARQTVLF RERLAKGETL
DQLLPEAFAT VREASKRTLG QRHYDVQIIG GIVLHRGEIA EMRTGEGKTL VATLACYLNA
LEGKGVHVVT VNDYLAKRDA EQMGQVYRFL GLTVGVVMPN ISDEERRQAY LADITYATNN
ELGFDYLRDN MKYTREQMVQ RPFNYAIIDE VDSILIDEAR TPLIISGPTD DKSDLYIAID
QVVKKLGSDD YEIDEKQKNV VLTEEGTERA EQFLKADGLL PEGNLYDFEN TQIVHHLNQA
LRANLMFRRD VDYLVRNNKV VIIDEFTGRM MDGRRWSEGL HQAIEAKEGV QIEPENQTLA
SITFQNYFRL YPRIAGMTGT AATEATEFHQ IYKMNVVTIP TNLPVQRKDE NDQFYKNLED
KFRAIAKSIK EHAASGQPIL VGTVSIEKSE LLSEYLRHEG VPHKVLNARY HEMEAHIVAQ
AGRLGAVTIA TNMAGRGTDI QLGGNADFRI ADELREMTEG PERDAAIIRI KKEVAEEKQK
VLDAGGLFVL GTERHESRRI DNQLRGRSGR QGDPGLSRFY LSLDDDLLRI FGSQTMFAKM
MNKSLADGEA IVSPIMSKAI ETAQRKVEAR NYDIRKQVVE YDDVMNDQRK VIYEQRATVM
DAESVNDLVE EMREDTIADL VSETCPEDQY VEQWDIDQLK EKALDLLNLD LPVKEWQEEE
GIDSEIIAER ILEKSDELLA ERSKDIPPEQ WAGIQKNTLL QAIDHHWKEH LSVLDSLRQI
IHLRAYAQQT PINEYKHEAF ALFERMLISI REDVTRNLSR IELFQPSFEL SELPEFFKNS
PEIMAALEEQ EKLLFETTVD GQNQPQDDQI TVNQMAAQQG AAAQTDSLSD ADPAHWVGKI
SRNAPCPCGS GKRYKHCHGA FDSKN
