SECA1_CHLCH
ID SECA1_CHLCH Reviewed; 1017 AA.
AC Q3ARU5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=Cag_1018;
OS Chlorobium chlorochromatii (strain CaD3).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=340177;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CaD3;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Chlorobium chlorochromatii CaD3.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000108; ABB28280.1; -; Genomic_DNA.
DR RefSeq; WP_011362045.1; NC_007514.1.
DR AlphaFoldDB; Q3ARU5; -.
DR SMR; Q3ARU5; -.
DR STRING; 340177.Cag_1018; -.
DR PRIDE; Q3ARU5; -.
DR EnsemblBacteria; ABB28280; ABB28280; Cag_1018.
DR KEGG; cch:Cag_1018; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_0_0_10; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
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 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; Translocase;
KW Translocation; Transport; Zinc.
FT CHAIN 1..1017
FT /note="Protein translocase subunit SecA 1"
FT /id="PRO_0000320770"
FT REGION 978..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 161..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 661
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 1003
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 1005
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 1014
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 1015
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 1017 AA; 116092 MW; A56863CE6D33977C CRC64;
MLKIFEKLFG SKHEKDVKKI QPTIQRINEL QRALASLSDE QLRQKGRELK QKVRGVLEPM
ELEQQKLFHQ LDSPNISLDE AESVNNKLDD LAVAYETATA SVLEEILPDT FALVKETCAR
LKGHTYNVMG RQFVWNMVPY DVQLIGGIVL HSGKIAEMQT GEGKTLVSTL PTFLNALTGR
GVHVVTVNDY LAQRDKEWME PLFAFHNLSV GVILTSMHPA LRRAQYLCDI TYGTNNELGF
DYLRDNMANT PEEMVQRKFY YAIVDEVDSV LIDEARTPLI ISGPVPNADN SKFQEIKPWI
EQLVRAQQQQ IAAWLGDAET RMKTNATDPE AGLALLRVKR GQPKNSRFIK MLSQQGVAKL
VQITENEYLK DNSSRMHEVD DALFYAVDEK ANTIDLTDKG RDFLSKLSHQ DSDIFLLPDV
GTEIATIESN AALSTNDKIQ HKDALYRLFS DRSERLHNIS QLLKAYSLFE RDDEYVVQNG
QVMIVDEFTG RILPGRRYSD GLHQAIEAKE NVKIEGETQT MATITIQNFF RLYKKLAGMT
GTAETEASEF YEIYKLDVVV IPTNASVVRK DMDDLVYKTR REKYNAIAQK VEELQKRGQP
VLVGTTSVEV SETLSRMLRT RRIAHNVLNA KQNDREAEIV AEAGQKGTVT IATNMAGRGT
DIKLGDGVRE LGGLYILGSE RHESRRIDRQ LRGRAGRQGD PGESVFYVSL EDELMRLFGS
DRVIAVMDRL GHEEGDVIEH SMITKSIERA QKKVEEQNFA IRKRLLEYDD VLNQQREVIY
SRRKNGLLKE RLTSDILDLL KDYSDTIVKK YHKDFDTAGL EEQLMRDLSI EFQLDRATFE
REGIDAVVDK VYETALTFYR RKEESLPADI MCQIEKYAVL TVIDQRWREH LREIDSLREG
INLRAYGQKD PLIEYKQEAF RLFITLLKEI EAETLSLAFK LFPIDPEEQQ QIEERQRQSA
IRQEKLVAQH DVAESFVGLN DDDEPLPAQP ITTEQKPGRN DLCPCGSGKK YKACCGQ
