SECA_CHLFF
ID SECA_CHLFF Reviewed; 969 AA.
AC Q256C7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=CF0089;
OS Chlamydia felis (strain Fe/C-56) (Chlamydophila felis).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=264202;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fe/C-56;
RX PubMed=16766509; DOI=10.1093/dnares/dsi027;
RA Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H.,
RA Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H., Fukushi H.,
RA Hattori M., Kuhara S., Shirai M.;
RT "Genome sequence of the cat pathogen, Chlamydophila felis.";
RL DNA Res. 13:15-23(2006).
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; AP006861; BAE80861.1; -; Genomic_DNA.
DR RefSeq; WP_011457646.1; NC_007899.1.
DR AlphaFoldDB; Q256C7; -.
DR SMR; Q256C7; -.
DR STRING; 264202.CF0089; -.
DR KEGG; cfe:CF0089; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_0; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000001260; 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..969
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000073470"
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; 111009 MW; E006EA373210EA7A CRC64;
MLDFLKRFFG SSQERTLKKF QKLVDKVNLY DEMLAPLSDE ELRNKTGELK KRYQEGESLD
DMLPEAYAVV KNVCRRLTGT PVEVSGYHQN WDMVPYDVQV LGAIAMHKGF ITEMQTGEGK
TLTAVMPLYL NALTGKPVHL VTVNDYLAQR DCEWVGSILR WLGLTTGVLI SGSPLEKRKE
IYRCDVVYGT ASEFGFDYLR DNSIATSVDE QVGRGFYFAI IDEVDSILID EARTPLIISG
PGEKHNPVYF ELKDKVAELV QLQRELCNQL ALEARRGLEH FLDMDILPKD KKVIEGISEF
CRSLWLVSKG MPLNRVLRRV REHPDLRAMI DKWDTYYHAE QNKEESIEKL SQLYIIVDEH
NNDFELTDRG MQQWVEKAGG SAEDFVMIDM GHEYALIDSD ESLSPTDKIN RKIAVSEEDT
QRKARAHGLR QLLRAHLLME RDVDYIVRND QIVIIDEHTG RPQPGRRFSE GLHQAIESKE
HVTIRKESQT FATITLQNFF RLYEKLAGMT GTAITESKEF KEIYNLYVLQ VPTFKTCLRI
DHNDEFYMTE REKYHAIVNE IARIHKDGNP ILIGTESVEV SEKLSRILKQ NRIEHTVLNA
KNHAQEAEII AAAGKLGAVT VATNMAGRGT DIKLDEEAVV VGGLHVIGTS RHQSRRIDRQ
LRGRCARLGD PGAAKFFLSF EDRLMRLFAS PKLNALIRHF RPPEGEAMSD PMFNKLIETA
QKRVEARNYT IRKHTLEYDD VMNKQRQTIY AFRNEVLRSE DIFALAKESI NHVALMIASL
IMSREHPAGH SLPILEEWMN YSFPLQLNIE ELRRLPSLDA IAEKVADELT GAFQNKFSSM
VEEITAAAGN DVDANGICKD IIRSVMIMHI DEQWKIHLVD MDLLRSEVGL RTVGQKDPLL
EFKHESFLLF ESLIRDIRIA IVKHLFRLEL TMTREQRPQN VIPVVATSFQ NDENFGPMEL
TIISDSDDE
