SECA_CYTH3
ID SECA_CYTH3 Reviewed; 1118 AA.
AC Q11YU5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-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=CHU_0128;
OS Cytophaga hutchinsonii (strain ATCC 33406 / DSM 1761 / CIP 103989 / NBRC
OS 15051 / NCIMB 9469 / D465).
OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC Cytophaga.
OX NCBI_TaxID=269798;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33406 / DSM 1761 / CIP 103989 / NBRC 15051 / NCIMB 9469 / D465;
RX PubMed=17400776; DOI=10.1128/aem.00225-07;
RA Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C., Gilna P.,
RA Han C.S., Lucas S., Misra M., Myers G.L., Richardson P., Tapia R.,
RA Thayer N., Thompson L.S., Brettin T.S., Henrissat B., Wilson D.B.,
RA McBride M.J.;
RT "Genome sequence of the cellulolytic gliding bacterium Cytophaga
RT hutchinsonii.";
RL Appl. Environ. Microbiol. 73:3536-3546(2007).
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; CP000383; ABG57421.1; -; Genomic_DNA.
DR RefSeq; WP_011583537.1; NZ_FPJX01000016.1.
DR AlphaFoldDB; Q11YU5; -.
DR SMR; Q11YU5; -.
DR STRING; 269798.CHU_0128; -.
DR EnsemblBacteria; ABG57421; ABG57421; CHU_0128.
DR KEGG; chu:CHU_0128; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_10; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000001822; 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; Reference proteome; Translocase;
KW Translocation; Transport.
FT CHAIN 1..1118
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000320788"
FT REGION 1034..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 194..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 693
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 1118 AA; 127579 MW; 8CA965D8A976516D CRC64;
MLGILAKLFG TKSGRDIKKL QPLVERINEE FQKLHALDDN QLRAQTDKIK GIIDADLSGI
DKQIKEHHDK IAANPDLSID EKEVVFQAID KLELERNKEL EKVLEKVLPQ AFAVVKDTAR
RWKENGKLTV TATPMDIELA SRKKNVQIIG STAEWSSKWL AAGTEVTWEM QHFDVQLIGG
MVLHHGKISE MGTGEGKTLV ATLPAYLNAL ARRGVHVVTV NDYLAKRDSE WMAPLFEFHG
ISVDCIDKYQ PNSEERRKAY RADITYGTNN EFGFDYLRDN MATDKDDLVQ RGHHYAMVDE
VDSVLIDDAR TPLIISGPVP KGDQHEFAEL KPRIQRVLEE QKKLINTYLV EAKRYIAAGK
EKEAGLELLR AHRGYPGYKP LIKQLSETGI KSILQKTENE YMAENNKRMP EVDLPLYFVI
DEKHNQVDFT EKGVDFITGE QEDPTLFVLP DIGSELAKIE KDKSISDQER MEQTEKLLSD
YSIKQERIHT LQQLLKAYTL FEKDTDYVIM DGKVKIVDEQ TGRIMDGRRY SDGLHQALEA
KENVRVEEAT QTYATITLQN YFRMYHKLSG MTGTAETEEA EFQQIYNLDV VVVPTNRSIA
RLDEQDKVYK TTREKYNAVA DEIVELTEKG RPVLVGTTSV DISELLSRML KMRNIKHQVL
NAKLHAKEAD VVAEAGKPGT VTIATNMAGR GTDIKLTAEA KASGGLAIIG TERHESRRVD
RQLRGRAGRQ GDPGSSQFFV SLEDNLMRLF GSDRIAKFMD RMGYKEGEVI QHSMISNSIE
RAQKKVEENN FGQRKRLLEY DNVMNSQRVV IYKRRKNALY GERLKLDILN MIFDLCEDMV
FGAYTTKNYD NFKLRSISVF GVIPDITEEV FNKATAETLV KSFYEEVLAH YEQKIKFVKE
KTQPTFNELQ LTRGETIENI VIPFTDGKRN INIIAPLKEL AQSDSRALEQ AIERYITLAV
IDMHWKDHLR EMDELKQSVQ NAAYEQKDPL LVYKFEGFEL FKKFVYTVNA DIVSFLFKAD
IPKQDTVPVR ELKQQPVQQP KYRETKDEAG SAFGGGNANQ QVEEAVAPPK AEPLRSQKIA
NRNDKVSVQY MDGSVKRDIK YKAVEDDLLS NKCVLIEE
