SECA_CHLL2
ID SECA_CHLL2 Reviewed; 1027 AA.
AC B3ECJ8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-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=Clim_1206;
OS Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290315;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 245 / NBRC 103803 / 6330;
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., Ovchinnikova G., Zhao F., Li T., Liu Z.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium limicola DSM 245.";
RL Submitted (MAY-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; CP001097; ACD90273.1; -; Genomic_DNA.
DR RefSeq; WP_012466150.1; NC_010803.1.
DR AlphaFoldDB; B3ECJ8; -.
DR SMR; B3ECJ8; -.
DR STRING; 290315.Clim_1206; -.
DR EnsemblBacteria; ACD90273; ACD90273; Clim_1206.
DR KEGG; cli:Clim_1206; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_0_0_10; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000008841; 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; Reference proteome;
KW Translocase; Translocation; Transport; Zinc.
FT CHAIN 1..1027
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000144988"
FT REGION 981..1027
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 1011
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 1013
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 1022
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 1023
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 1027 AA; 117012 MW; 094BA1AF0F4AAE13 CRC64;
MLKIFEKIFG SKHDKDIKKI QPVIQRINEL QLSFQSLSDD GLKEMGLQLR STARGALRPL
EEKKQELLSK LSTPDIPLEE ADRINDELDT LSEEYEKATV SVLEEILPDT FALVKDTCRR
LKGHVYTVMG HDMTWDMVPY DVQLIGGMVL HSGRISEMAT GEGKTLVSTL PIFLNALTGR
GVHVVTVNDY LAQRDKEWMT PVFEYHGLSV GVILNTMHPF ERREQYRCDI TYGTNNEFGF
DYLRDNMAGS VEEMVQRDFY FAIVDEVDSV LIDEARTPLI ISGPVPNADN SKFQEIKPWI
DQLVRNQQQL VASYLTDAEK ILKTKPGDFD AGLALLRVKR GQPKNSRFIK MLSQQGLAKL
VQGTENEFLK DNASRMHEVD DELFYAVDEK AGTIDLTDKG RDFLSRLSHQ DSDIFLLPDV
GSEIAIIESN ASLSAAEKVK QKDAVYRLFA DRSERLHNIS QLLKAFSLFE RDDEYVVQDG
KVMIVDEFTG RILPGRRYSD GLHQAIEAKE NVRIEGETQT MATITIQNFF RLYKKLAGMT
GTAETEASEF YEIYKLDVVV IPTNRPIVRK DMDDLVYKTR REKYNAVVEK VEELQKKGQP
VLVGTASVEV SETLSRMLRG KRIAHSVLNA KQHDREAEIV AAAGQKGAVT IATNMAGRGT
DIKLGSGVRE LGGLFILGSE RHESRRIDRQ LRGRAGRQGD PGESVFFVSL EDELMRLFGS
ERVISVMDRL GHEEGDVIEH TMITKSIERA QKKVEEQNFA IRKRLLEYDD VLNQQRDVIY
TRRKNGLQKE RLTSDIFDLL RDYCDMVVKK YEKAFDPEEL EERLLRELSV EFRPESGLFD
REGAKGIADK LYETALAFYS RKEKEIPEEI MGQIEKYAVL SVIDKKWREH LREIDSLREG
INLRAYGQKD PLLEYKQEAF RLFVVLLQEI ELETLSLAFK LFPVNPDEAR EIEARQKKEA
LRQEKLVAQH QAAESIYQHI EESGTSNADN AGDNGPQTVI AEKKPGRNDL CPCGSGKKYK
NCHGQQP
