SECA_CHLMU
ID SECA_CHLMU Reviewed; 968 AA.
AC Q9PLM5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
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=TC_0074;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
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).
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; AE002160; AAF38956.1; -; Genomic_DNA.
DR PIR; G81743; G81743.
DR RefSeq; WP_010229296.1; NZ_CP027217.1.
DR AlphaFoldDB; Q9PLM5; -.
DR SMR; Q9PLM5; -.
DR STRING; 243161.TC_0074; -.
DR EnsemblBacteria; AAF38956; AAF38956; TC_0074.
DR GeneID; 1245603; -.
DR KEGG; cmu:TC_0074; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_0; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000000800; 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; 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..968
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000109582"
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 968 AA; 110513 MW; 187B5536F547D3FC CRC64;
MMDFLKRFFG SSQERILKRF QKLVEEVNAC DEKFSSLSDD ELREKTPQLK RRYQEGESLD
KLLPEAYGIV KNVCRRLAGT PVEVSGYHQQ WDMVPYDVQI LGGIAMHKGF ITEMQTGEGK
TLTAVMPLYL NALTGKPVHL VTVNDYLAQR DCEWVGSVLR WLGLTTGVLV SGIPPERRKA
IYQCDVVYGT ASEFGFDYLR DNSIATRKEE QVGRGFYFAI IDEVDSVLID EARTPLIISG
PGEKHNPVYF ELKDKVAELV HFQREMCNHI AAEARKTLDP FLGMDVLPKD RKIMEGISEA
CRALWLVSKG MPLNRVLRRV REHPDLRAMV DKWDVFYHAE QNKEECLERL SSLYIVVDEH
NNDFELTDKG MQQWIEKIGG AAEDFVMMDM GHEYALIEED TTLSPEDKLN RKIAVSEKDT
QRKARAHGLR QLLRAHLLME RDIDYIVRDD QIVIIDEHTG RPQAGRRFSE GLHQAIEAKE
HVTIRKESQT FATVTLQNFF RLYEKLAGMT GTAITESREF KEIYNLYVLQ VPTFKPCLRI
DHNDAFYMTE REKYQAIVAE IISAHRSGKP ILIGTESVEV SEKLSRILRQ NRIHHTVLNA
KNHAQEAEII AGAGKVGAVT VATNMAGRGT DIKLDKEAVA AGGLYVIGTS RHQSRRIDRQ
LRGRCARLGD PGAAKFFLSF EDRLMRLFAS PKLNTLIRHF RPPEGEAMSD PMFDRLIETA
QKRVEGRNYT IRKHTLEYDD VMNKQRQTIY AFRNDVLHAD DLFIVAREQI EHVSLALAFL
ILKDARADHC SLPKVEEWLS YSFPVKLDDQ EIRRLGNVDA VADYIGGLLI EAFDAKFSSM
LTEFTEIIGS ASGAQGVCND ILRSVIISHI DEEWKVHLMD MDLLRSEVGL RSVGQKDPLI
EFKNESFLLF EGLIRDIRIA IVKHLFALEL SLTRSDRPDN AIPTVATAFH NHDNFRPMEL
TIIGEEEN
