ID A0A563D7R6_9FLAO Unreviewed; 1105 AA.
AC A0A563D7R6;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Protein translocase subunit SecA {ECO:0000256|HAMAP-Rule:MF_01382, ECO:0000256|RuleBase:RU003874};
DE EC=7.4.2.8 {ECO:0000256|HAMAP-Rule:MF_01382};
GN Name=secA {ECO:0000256|HAMAP-Rule:MF_01382,
GN ECO:0000313|EMBL:TWP26137.1};
GN ORFNames=ETU09_10580 {ECO:0000313|EMBL:TWP26137.1};
OS Apibacter muscae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Apibacter.
OX NCBI_TaxID=2509004 {ECO:0000313|EMBL:TWP26137.1, ECO:0000313|Proteomes:UP000319499};
RN [1] {ECO:0000313|EMBL:TWP26137.1, ECO:0000313|Proteomes:UP000319499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AL1 {ECO:0000313|EMBL:TWP26137.1,
RC ECO:0000313|Proteomes:UP000319499};
RA Park R.;
RT "Apibacter muscae sp. nov.: a novel member of the house fly microbiota.";
RL Submitted (FEB-2019) 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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01382}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01382};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01382};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01382}. Cytoplasm
CC {ECO:0000256|HAMAP-Rule:MF_01382}. Note=Distribution is 50-50.
CC {ECO:0000256|HAMAP-Rule:MF_01382}.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000256|ARBA:ARBA00007650,
CC ECO:0000256|HAMAP-Rule:MF_01382, ECO:0000256|RuleBase:RU003874}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TWP26137.1}.
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DR EMBL; SELH01000026; TWP26137.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A563D7R6; -.
DR OrthoDB; 9805579at2; -.
DR Proteomes; UP000319499; Unassembled WGS sequence.
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: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; cd17928; DEXDc_SecA; 1.
DR CDD; cd18803; SF2_C_secA; 1.
DR Gene3D; 1.10.3060.10; Helical scaffold and wing domains of SecA; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.90.1440.10; SecA, preprotein cross-linking domain; 1.
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 NCBIfam; TIGR00963; secA; 1.
DR PANTHER; PTHR30612:SF0; CHLOROPLAST PROTEIN-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR30612; SECA INNER MEMBRANE COMPONENT OF SEC PROTEIN SECRETION SYSTEM; 1.
DR Pfam; PF21090; P-loop_SecA; 2.
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; SSF81886; Helical scaffold and wing domains of SecA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF81767; Pre-protein crosslinking domain of SecA; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01312; SECA; 1.
DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01382}; Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01382}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01382};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01382};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01382};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW Rule:MF_01382}; Reference proteome {ECO:0000313|Proteomes:UP000319499};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW Rule:MF_01382};
KW Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW Rule:MF_01382};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01382}.
FT DOMAIN 5..772
FT /note="SecA family profile"
FT /evidence="ECO:0000259|PROSITE:PS51196"
FT DOMAIN 179..338
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 619..788
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT COILED 16..103
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT BINDING 195..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT BINDING 694
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ SEQUENCE 1105 AA; 126701 MW; 8C41418203BE3FF2 CRC64;
MNILNSILKL FVGDKHKKDL ELLNKYLEKI KNEEEQIATL SIDQLRYKTI EFKEKINDAT
QEIRTKINDL KQKTQTTEDV EEKEKFYAEI EKLEKESYEI EEKVLEEILP QAYAVIKETA
KRFTENSTIE ASVTDFDKEL ANAKEYVTIN GEKSIWKNNW NAAGKDVQWD MIHYDVQYIG
GTVLHKGKIA EMATGEGKTL VGTLPMYLNA LTGRGVHVVT VNDYLAKRDS AWMAPIFEFH
GLKVDCIDNH QPNSESRRQA YLSDIVYGTN NEFGFDYLRD NMANSPSDLV QRELNYAIVD
EVDSVLIDDA RTPLIIAGPV PQGDKQEYQI LKPVVESIFT VQKNELTKIF QEAKQLLANG
DKKLGGQKLY QVFRGLPKFK PLIKFLSEEG NKAILLKAEA YFISDNNRMM PEADKDLYFA
IDEKNNQVEL TDKGIEFLSK GNEDPHFFML EDLGSAIADI ESKNLPKEEE HKEKEEFLRE
FAIKSERIHS LNQLLKAYTL FEKDIEYVVM DGQVKIVDEQ TGRIMEGRRY SDGLHQALEA
KENVKIEAAT QTFATITLQN YFRMYNKLAG MTGTAETEAG EFWEIYKLDV VAIPTNKPVV
RKDHQDLVYK TNREKFNAVL NEVIRLSQEE KRPVLVGTTS VEVSELLSKA LKMRKIPHNV
LNAKLHKKEA EVVAEAGKPG VVTIATNMAG RGTDIKLIDE VKDAGGLAII GTERHDSRRV
DRQLRGRAGR QGDPGSSQFY VSLEDNLMRL FGSDRIAKMM DRLGHKEGDV IQHSMISNSI
ERAQKKVEEN NFGIRKRLLE YDDVMNKQRE VIYSRRKNAL FGEKLSIDIA NMIFDTAALI
VKENKSNRDF KNFEFELATT FAMDTPMDSA EFNSLNEADI TQKVFEQAEA LYKEKLENTA
EQLYPTVSNV FLSPNRSYKN ISVPFTDGSK VINVTTNLEE AYNSGGKALL KDFEKSITLA
IIDENWKDHL REMDELRKSA QSAVWEQKDP LVIYKQESFK LFRDMLDKTN KEIISFLFKG
GLPIEANNTT IHEAKEVKQK MVESRNFEEN QEEEAKDREI KEPLRVNKIG RNELVTIRNL
RTGEVKNLKF KQAQPYIDEG WMVED
//
