SECA2_STAHJ
ID SECA2_STAHJ Reviewed; 796 AA.
AC Q4L9N5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Protein translocase subunit SecA 2 {ECO:0000255|HAMAP-Rule:MF_01382};
DE EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382};
GN Name=secA2 {ECO:0000255|HAMAP-Rule:MF_01382}; OrderedLocusNames=SH0331;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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 -!- 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; AP006716; BAE03640.1; -; Genomic_DNA.
DR RefSeq; WP_011274659.1; NC_007168.1.
DR AlphaFoldDB; Q4L9N5; -.
DR SMR; Q4L9N5; -.
DR STRING; 279808.SH0331; -.
DR EnsemblBacteria; BAE03640; BAE03640; SH0331.
DR KEGG; sha:SH0331; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_2_9; -.
DR OMA; QRIDYPD; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000000543; 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: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; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000185; SecA.
DR InterPro; IPR022490; SecA2.
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; 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; TIGR03714; secA2; 1.
DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Cytoplasm; Membrane; Nucleotide-binding;
KW Protein transport; Translocase; Translocation; Transport.
FT CHAIN 1..796
FT /note="Protein translocase subunit SecA 2"
FT /id="PRO_0000318434"
FT BINDING 84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 102..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 496
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 796 AA; 91461 MW; 938CE8667A604241 CRC64;
MANQVSNVIN SMRLKRLQKQ LVAVNRLSDQ MRNCSDEALQ AKTADFKQRL EKRETTLDKL
LPEAYATIRE ASKRVLGMYP KDVQVMGAIV MHQGNIAEMQ TGEGKTLTAT MPLYLNALTG
KSAFLITTND YLANRDFQEM RPLYEWLGLT ASLGFVDIPD YEYAENEKQM LYNHDIIYTT
NGRLGFDYLF DNLADHINAK YLPELNFAII DEVDSIILDA AQTPLVISGA PRVQSNLFHI
IKMFVETLVE DEHFKLNVNK KEVWLTDEGI DVANHYFKVN NIYLPQYFDL VRVINLSLRA
KYLFKDNLDY FIYNGEVVLI DRITGRMLPG TKLQSGLHQA IEAKEGVELS QDLSVMATIT
FQNLFKLFNG FSGMTGTGKL GEKEFFDLYS KLVVEIPTNH PIIRNDKEDR VYAKSDEKNK
AILEKVKEIH ATKQPVLLIT RTAEAAEYFS TQLFKDNIPN NLLIAQNVAK EAQMIAEAGQ
LGAVTVSTSM AGRGTDIKLG SGVYELGGLA VIINEHMENS RVDRQLRGRS GRQGDPGVSQ
IYVSLDDYIV KRWSNSKLAE NKKLKDVDPD KLQDSPFFRR RVRGIVSKAQ RVSEETSMMA
REMANEFEKS IGIQRDRVYE ERNRILETSD FSAFDFDSLA RDVFDYDLRT KHIHNKDDII
NYIYEQLSFS FKDDAISQQI QTREQTIDYL VQQFNKQLKE NMKIANNDYF KLRFFQKAIL
KAIDVEWINQ VDQLQQLKAS VNNRQNGQRN AIFEYHKVAL ETYEMMLINI KRATIRNLCL
SILTFDKDQD LVVHFP
