SECA_CHLTR
ID SECA_CHLTR Reviewed; 969 AA.
AC O84707;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=CT_701;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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 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; AE001273; AAC68296.1; -; Genomic_DNA.
DR PIR; G71482; G71482.
DR RefSeq; NP_220220.1; NC_000117.1.
DR RefSeq; WP_010725308.1; NC_000117.1.
DR AlphaFoldDB; O84707; -.
DR SMR; O84707; -.
DR STRING; 813.O172_03875; -.
DR EnsemblBacteria; AAC68296; AAC68296; CT_701.
DR GeneID; 884489; -.
DR KEGG; ctr:CT_701; -.
DR PATRIC; fig|272561.5.peg.772; -.
DR HOGENOM; CLU_005314_0_0_0; -.
DR InParanoid; O84707; -.
DR OMA; MVHYDVQ; -.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015462; F:ABC-type protein transporter activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
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 GO; GO:0043952; P:protein transport by the Sec complex; IBA:GO_Central.
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; 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; 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 Nucleotide-binding; Protein transport; Reference proteome; Translocase;
KW Translocation; Transport.
FT CHAIN 1..969
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000109584"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 117..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 631
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 969 AA; 110358 MW; 2D551C2269EE86BE CRC64;
MMDFLKRFFG SSQERILKRF QKLVEEVNAC DEKFSSLSDD ELRKKTPQLK QRYQDGESLD
KLLPEAYGVV KNVCRRLAGT PVEVSGYHQQ WDMVPYDVQI LGAIAMHKGF ITEMQTGEGK
TLTAVMPLYL NALTGKPVHL VTVNDYLAQR DCEWVGSVLR WLGLTTGVLV SGSPPEKRKA
IYQCDVVYGT ASEFGFDYLR DNSIATRKEE QVGRGFYFAI IDEIDSVLID EARTPLIISG
PGEKHNPVYF ELKDRVAELV YFQREMCNHI AIEARKVLDP FLGTDVLPKD KKVVEAISEA
CRALWLVSKG MPLNRVLRRV REHPDLRAMI DKWDVFYHAE QNKEQCLEKL SSLYIVVDEH
NNDFELTDKG MLQWIEKIGG AAEDFVMMDM GHEYALIEED ATLSPADKLN RKIAVSEKDT
QRKARAHGLR QLLRAHLLME KDIDYIVRDD QIVIIDEHTG RPQSGRRFSE GLHQAIEAKE
HVTIRKESQT FATVTLQNFF RLYEKLAGMT GTAITESREF KEIYSLYVLQ VPTFKPCLRI
DHNDAFYMTE REKYQAIVAE IISAHRSGKP ILIGTESVEV SEKLSRILRQ NRINHTVLNA
KNHAQEAEII AGAGKVGAVT VATNMAGRGT DIKLDEEAVA AGGLYVIGTS RHQSRRIDRQ
LRGRCARLGD PGAAKFFLSF EDRLMRLFAS PKLNTLIRHF RPPEGEAMSD PMFDRLIETA
QKRVEGRNYT IRKHTLEYDD VMNKQRQTIY AFRNDVLHAE DLFVVAKEQI EHVALALAFL
ILKDAHADHC SLPKIEEWLS YSFPVKLDDQ EIRRLGDVDA VADYIGDLLI EAFDVKFSAM
LAEFTEIIGS AANAQGICND ILRSVIISHI DEEWKVHLVD MDLLRSEVGL RSVGQKDPLI
EFKNESFLLF EGLIRDIRIA IVKHLFALEL SLTRSDRPDN AIPTVATAFH NHDNFRPMEL
TIVGEEEES
