SECA_CHLPN
ID SECA_CHLPN Reviewed; 970 AA.
AC Q9Z765; Q9JQE5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 135.
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};
GN OrderedLocusNames=CPn_0841, CP_1028, CpB0870;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) 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 -!- 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; AE001363; AAD18979.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38804.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA99049.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98799.1; -; Genomic_DNA.
DR PIR; A72028; A72028.
DR PIR; G86595; G86595.
DR RefSeq; NP_225036.1; NC_000922.1.
DR RefSeq; WP_010883478.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z765; -.
DR SMR; Q9Z765; -.
DR STRING; 115711.CP_1028; -.
DR EnsemblBacteria; AAD18979; AAD18979; CPn_0841.
DR EnsemblBacteria; AAF38804; AAF38804; CP_1028.
DR GeneID; 45050895; -.
DR KEGG; cpa:CP_1028; -.
DR KEGG; cpj:secA_2; -.
DR KEGG; cpn:CPn_0841; -.
DR KEGG; cpt:CpB0870; -.
DR PATRIC; fig|115713.3.peg.921; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_0; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; 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; -; 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; Translocase; Translocation;
KW Transport.
FT CHAIN 1..970
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000109583"
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 970 AA; 111092 MW; 9FA9C2A88C3C5DC0 CRC64;
MLGFLKRFFG SSQERILKKF QKLVDKVNIY DEMLTPLSDD ELRNKTAELK QRYQNGESLD
SMLPEAYGVV KNVCRRLAGT PVEVSGYHQR WDMVPYDVQI LGAIAMHKGF ITEMQTGEGK
TLTAVMPLYL NALTGKPVHL VTVNDYLAQR DCEWVGSVLR WLGLTTGVLV SGTLLEKRKK
IYQCDVVYGT ASEFGFDYLR DNSIATRLEE QVGRGYYFAI IDEVDSILID EARTPLIISG
PGEKHNPVYF ELKEKVASLV YLQKELCSRI ALEARRGLDS FLDVDILPKD KKVLEGISEF
CRSLWLVSKG MPLNRVLRRV REHPDLRAMI DKWDVYYHAE QNKEESLERL SELYIIVDEH
NNDFELTDKG MQQWVEYAGG STEEFVMMDM GHEYALIEND ETLSPADKIN KKIAISEEDT
LRKARAHGLR QLLRAQLLME RDVDYIVRDD QIVIIDEHTG RPQPGRRFSE GLHQAIEAKE
HVTIRKESQT LATVTLQNFF RLYEKLAGMT GTAITESREF KEIYNLYVLQ VPTFKPCLRI
DHNDEFYMTE REKYHAIVNE IATIHGKGNP ILVGTESVEV SEKLSRILRQ NRIEHTVLNA
KNHAQEAEII AGAGKLGAVT VATNMAGRGT DIKLDNEAVI VGGLHVIGTT RHQSRRIDRQ
LRGRCARLGD PGAAKFFLSF EDRLMRLFAS PKLNTLIRHF RPPEGEAMSD PMFNRLIETA
QKRVEGRNYT IRKHTLEYDD VMNKQRQAIY AFRHDVLHAE SVFDLAKEIL CHVSLMVASL
VMSDRQFKGW TLPNLEEWIT SSFPIALNIE ELRQLKDTDS IAEKIAAELI QEFQVRFDHM
VEGLSKAGGE ELDASAICRD VVRSVMVMHI DEQWRIHLVD MDLLRSEVGL RTVGQKDPLL
EFKHESFLLF ESLIRDIRIT IARHLFRLEL TVEPNPRVNN VIPTVATSFH NNVNYGPLEL
TVVTDSEDQD
