SECA_STREM
ID SECA_STREM Reviewed; 842 AA.
AC B4U176;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Sez_0367;
OS Streptococcus equi subsp. zooepidemicus (strain MGCS10565).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=552526;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGCS10565;
RX PubMed=18716664; DOI=10.1371/journal.pone.0003026;
RA Beres S.B., Sesso R., Pinto S.W.L., Hoe N.P., Porcella S.F., Deleo F.R.,
RA Musser J.M.;
RT "Genome sequence of a lancefield group C Streptococcus zooepidemicus strain
RT causing epidemic nephritis: new information about an old disease.";
RL PLoS ONE 3:E3026-E3026(2008).
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 membrane {ECO:0000255|HAMAP-Rule:MF_01382};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01382};
CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}. Cytoplasm
CC {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50-50.
CC {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; CP001129; ACG61743.1; -; Genomic_DNA.
DR RefSeq; WP_012515019.1; NC_011134.1.
DR AlphaFoldDB; B4U176; -.
DR SMR; B4U176; -.
DR EnsemblBacteria; ACG61743; ACG61743; Sez_0367.
DR KEGG; sez:Sez_0367; -.
DR HOGENOM; CLU_005314_3_0_9; -.
DR OMA; MVHYDVQ; -.
DR Proteomes; UP000001873; 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 membrane; Cytoplasm; Membrane; Metal-binding;
KW Nucleotide-binding; Protein transport; Translocase; Translocation;
KW Transport; Zinc.
FT CHAIN 1..842
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000145064"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 103..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 825
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 827
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 836
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 837
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 842 AA; 95307 MW; 18955C422944BD03 CRC64;
MSNILRKVIE NDKGELRKLE KIAKKVESYA DYMESLSDKD LQAKTPEFKQ RYQNGETLEQ
LLPEAFAVVR EAARRVLGLY PYRVQIMGGI VLHNGDVPEM RTGEGKTLTA TMPVYLNALA
GKGVHVITVN EYLSTRDATE MGEVYSWLGL SVGINLAAKS PAEKREAYLC DITYSTNSEV
GFDYLRDNMV VRQEDMVQRP LNFALVDEVD SVLIDEARTP LIVSGAVSSE TNQLYIRADM
FVKTLDSVDY IIDVPTKTIG LSDSGIDKAE SYFNLSNLYD IENVALTHFV DNALRANYIM
LLDIDYVVSE EGEILIVDQF TGRTMEGRRF SDGLHQAIEA KEGVRIQEES KTSASITYQN
MFRMYKKLAG MTGTAKTEEE EFREVYNMRI IPIPTNRPIA RIDHTDLLYA TLNSKFKAVV
ADVKARYEKG QPVLVGTVAV ETSDLISKKL VEAGIPHEVL NAKNHFKEAQ IIMNAGQRGA
VTIATNMAGR GTDIKLGEGV RELGGLCVIG TERHESRRID NQLRGRSGRQ GDPGESQFYL
SLEDELMRRF GTDRIKAFLD RMNHDDEDIV IKSRMLSRQV ESAQKRVEGN NYDTRKQVLQ
YDDVMREQRE IIYANRRDVI TANRDLGPEI KAMIKRTIDR AVDAHSRTNR KDAIDAIVTF
ARTSIVPEET IGAKELRGLK DDQIKDKLYQ RALEIYDKQL SKLRDQDAIL EFQKVLILMI
VDNKWTEHID ALDQLRNAVG LRGYAQNNPV VEYQSEGFKM FQDMIGAIEF DVTRTMMKAQ
IHEQERERAT QYATTTAAQN IQSQAIGADF DSSADFSRVE RNDACPCHSG KKFKNCHGRK
AF
