SECA_METC4
ID SECA_METC4 Reviewed; 970 AA.
AC B7KUB4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=Mchl_1756;
OS Methylorubrum extorquens (strain CM4 / NCIMB 13688) (Methylobacterium
OS extorquens).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=440085;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM4 / NCIMB 13688;
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., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Marx C., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium chloromethanicum
RT CM4.";
RL Submitted (DEC-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 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; CP001298; ACK82619.1; -; Genomic_DNA.
DR RefSeq; WP_015950414.1; NC_011757.1.
DR AlphaFoldDB; B7KUB4; -.
DR SMR; B7KUB4; -.
DR EnsemblBacteria; ACK82619; ACK82619; Mchl_1756.
DR KEGG; mch:Mchl_1756; -.
DR HOGENOM; CLU_005314_3_0_5; -.
DR OMA; MVHYDVQ; -.
DR BioCyc; MEXT440085:MCHL_RS08455-MON; -.
DR Proteomes; UP000002385; 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; Translocase;
KW Translocation; Transport; Zinc.
FT CHAIN 1..970
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000184238"
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 524
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 951
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 953
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 962
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 963
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 970 AA; 108921 MW; 81A9461DA8230979 CRC64;
MLGALAKKIF GSSNDRRVKG FRPRVAAINA LEPEISALSD EQLRARTQTF RDQLAAGTRL
DDLLVPAFAT VREAAKRVLG QRHFDVQMIG GMVLHESGIS EMKTGEGKTL VATLPVYLNA
LEGKGVHVIT VNDYLASRDA EWMGRVYRFL GLTVGTIVHG LDDGQRKEAY ACDITYGTNN
EFGFDYLRDN MKYELSQMTQ RGHHFAIVDE VDSILIDEAR TPLIISGPVD DRSELYVAVD
TVMPRLTPEH YDLDEKQRQV SLTEAGNEFI EEELRAEGIL KEGDLYDAHN VTIVHHVNQA
LRAHTLFTLD KDYIVKNDEV VIIDEFTGRM MQGRRYSEGL HQALEAKERV TIQPENQTLA
SITFQNYFRL YKKLAGMTGT ASTEADEFAE IYKLDVVDIP TNKEVERVDE DDEVYRTVEE
KYEAIIKEID KAHARHQPIL VGTGSIEKSE LIGELLKKAG YTLLDYSDPN ALTDVYKAAR
ENRVTKRFAV LNARFHEQEA YIVAEAGVPG AITIATNMAG RGTDIKLGGN LEMRIEKELG
QMPEGPERAA AIEALKAEIA ENRAKVLASG EKADPEAGRK KDLPGGLYII GTERHESRRI
DNQLRGRSGR QGDPGRSKFY LSLKDDLMRI FGSDRMDGML QRLGLEQGEA IIHPWINKAI
EKAQQKVEAR NFDMRKNVLK YDNVMNDQRK VVFEQRRDLM GQDSVRETVD EMRHGVIDDF
VAVHIPENAY AEQWDAEGLK HRALDVLGLD LPIEEWVKEE GIADEEIRER LRKASDESYA
ARVERNGAEV MTYVEKQVVL QVLDHLWREH LVTLDHLRQV IGWRGFAQRD PLNEYKSEAF
ELFNGLVTAL REQVTAQLSH VEIMQQQPEG FADGGFESAG FSEPQLPPMF PEHRDPVTGE
NEFAFAGSGS DGGAGGAYGF AARELSADAA VLERNPDDAS TWGRVGRNEP CPCGSGKKYK
HCHGRFATEA
