ID   SECA_CHLP8              Reviewed;        1031 AA.
AC   B3QN61;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Cpar_0955;
OS   Chlorobaculum parvum (strain DSM 263 / NCIMB 8327) (Chlorobium vibrioforme
OS   subsp. thiosulfatophilum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=517417;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 263 / NCIMB 8327;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Zhao F., Li T., Liu Z., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobaculum parvum NCIB 8327.";
RL   Submitted (JUN-2008) 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; CP001099; ACF11364.1; -; Genomic_DNA.
DR   RefSeq; WP_012502197.1; NC_011027.1.
DR   AlphaFoldDB; B3QN61; -.
DR   SMR; B3QN61; -.
DR   STRING; 517417.Cpar_0955; -.
DR   EnsemblBacteria; ACF11364; ACF11364; Cpar_0955.
DR   KEGG; cpc:Cpar_0955; -.
DR   eggNOG; COG0653; Bacteria.
DR   HOGENOM; CLU_005314_3_0_10; -.
DR   OMA; MVHYDVQ; -.
DR   OrthoDB; 212453at2; -.
DR   Proteomes; UP000008811; 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   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..1031
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_1000144989"
FT   REGION          1001..1021
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         662
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
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"
FT   BINDING         1017
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         1026
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         1027
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   1031 AA;  117530 MW;  E444D5BFBC05E71C CRC64;
     MLKIFTKLFG SKHEKDVKKI KPIVDQINEL YGPLQSLSDE AFRNKGTELR KKVRDSLIPI
     EKNIADTEKK LDNPDLSHEE NEQLNDTLDN LRKEYETATA SILDEVLPET FALVKETCRR
     LKGHTYEVMG REMVWDMVPY DVQLIGGVVL HQGKIAEMAT GEGKTLVSTL PVFLNALTGR
     GVHVVTVNEY LAQRDMEWMR PVYEYHGLST GVILSGLYSH QRRNEYLCDI TWGTNSEFGF
     DYLRDNMAGT VEEMVQRDYY FAIVDEVDSV LIDEARTPLI ISGPVPNSDT DTKYREIKPW
     IEQIVRAQQN LVASLLGEAE KTLKTKPNDF DAGLALLRVK RGQPKNNRLS KMLSQTGVGK
     LIQSVENEYL KDNASRMHEV DEMLYYAVDE KANTIDLTDK GREFLSKLSH QDQDLFLLPD
     VGSEVAAIDA DANLQPSDKV RKKDEVYRLY AERSDSLHTI SQLLKAYTLF AKDDEYVVQD
     GQVNIVDEFT GRVLAGRRYS DGLHQAIEAK ENVKIEGETQ TMATITIQNF FRLYKKLAGM
     TGTAETEASE FFEIYKLDVV VIPTNKPIAR NDMDDLVYKT RREKYNAITS KVQELVAKGQ
     PVLVGTASVE VSETLSRMLR AKRIQHNVLN AKQHAREADI VAMAGQKGAV TIATNMAGRG
     TDIKLGEGIR EMGGLFILGS ERHESRRIDR QLRGRAGRQG DPGESIFYVS LEDQLMRLFG
     SERVISVMDR LGHEEGDVIE HSMITKSIER AQKKVEEQNF AIRKRLLEYD DVMNQQREVV
     YSRRRKALKM DRLTADIMDL LLDYCNTVVK KFHEANDPAG LEEQVMRELM VEFKPDPSAF
     EREPYEKSAE ELFKAASEFY HRKESDLPDD IMRQIEKYAV LSVIDQKWRE HLREIDGLRE
     GINLRAYGQK DPLLEYKQEA YKLFVDLLQE IEHETLSLAF KLFPITPEES EAIEARQRQQ
     AINQERLVAQ HKEAESAYEV SPNASVDSTM SMPGDEIVVQ QPIRAEQKPG RNDPCPCGSG
     KKYKNCCGTN E