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Database: UniProt
Entry: A9MHZ4_SALAR
LinkDB: A9MHZ4_SALAR
Original site: A9MHZ4_SALAR 
ID   A9MHZ4_SALAR            Unreviewed;      1295 AA.
AC   A9MHZ4;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN   OrderedLocusNames=SARI_02004 {ECO:0000313|EMBL:ABX21884.1};
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514 {ECO:0000313|EMBL:ABX21884.1, ECO:0000313|Proteomes:UP000002084};
RN   [1] {ECO:0000313|EMBL:ABX21884.1, ECO:0000313|Proteomes:UP000002084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980
RC   {ECO:0000313|Proteomes:UP000002084};
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC       {ECO:0000256|ARBA:ARBA00006474}.
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DR   EMBL; CP000880; ABX21884.1; -; Genomic_DNA.
DR   STRING; 41514.SARI_02004; -.
DR   KEGG; ses:SARI_02004; -.
DR   HOGENOM; CLU_001981_0_1_6; -.
DR   Proteomes; UP000002084; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR   CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR   Gene3D; 3.30.980.40; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR025199; FtsK_4TM.
DR   InterPro; IPR041027; FtsK_alpha.
DR   InterPro; IPR002543; FtsK_dom.
DR   InterPro; IPR018541; Ftsk_gamma.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR22683:SF41; DNA TRANSLOCASE FTSK; 1.
DR   PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
DR   Pfam; PF13491; FtsK_4TM; 1.
DR   Pfam; PF17854; FtsK_alpha; 1.
DR   Pfam; PF09397; FtsK_gamma; 1.
DR   Pfam; PF01580; FtsK_SpoIIIE; 1.
DR   SMART; SM00843; Ftsk_gamma; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50901; FTSK; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000002084};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        42..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        92..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        127..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        154..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        182..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          941..1154
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          373..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          663..719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          732..816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1209..1229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..474
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        676..691
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        696..710
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        764..782
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         958..965
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1295 AA;  141285 MW;  F1AF019294BF7915 CRC64;
     MSVLASGGKS LEPGEPFLSQ EYTEDKDVTL TKLSSGRRLL EALLILIALF AVWLMAALLS
     FNPSDPSWSQ TAWHEPIHNL GGAPGAWLAD TLFFIFGVMA YTIPVIIVGG CWFAWRHQST
     DDYIDYFAVS LRLIGVLALI LTSCGLAAIN ADDIWYFASG GVIGSLLSTT LQPLLHSSGG
     TITLLCIWAA GLTLFTGWSW VSIAEKLGGW LLNILTFASN RTRRDDTWVD DEEYEDEYDE
     ETDGVQRESR RARILRGALA RRKRLAAKFS NPRGRQTDAA LFSGKRMDDG EDIQYSARGV
     AADPDDVLFS GNRATQPEYD EYDPLLNGHS VAEPVAAAAA ATAVTQTWAT SADPVTQTPS
     MPEAVVAQPT VEWQPVPGPQ TGEPVIAPAP EGYPSHPQYA QPQAAQDAPW QQPAPVASAP
     KYAVSPAIAA EYESPAPQET QPQRQAPGVE QHWQPEPTHQ PTPVYQPDPV AAEPSHIPPV
     VEQPVVTEPE PVIEETRPAR PPLYYFEEVE EKRAREREQL AAWYQPIPEP IKETAPVKAA
     APVKPSVSAA PSIPPVEAVA AAAGIKSGAL AAGAAAAAPA FGLATSGAPR PQVKEGIGPQ
     LPRPNRVRVP TRRELASYGI KLPSQRIAEE KAREAERYQY ETGAQLTDEE IDAMHQDELA
     RQFAQSQQHR YGEAYQHDTQ QAEDDDTAAE AELARQFAAS QQQRYSGEQP AGAQPFSLDN
     LDFSPMKILV DEGPHEPLFT PGVMPESAPI QQPVAPQPQY QQPQQPVAPQ SQYQQPQQPA
     APQDSLIHPL LMRNGDSRPL QRPTTPLPSL DLLTPPPSEV EPVDTFALEQ MARLVEARLA
     DFRIKADVVN YSPGPVITRF ELNLAPGVKA ARISNLSRDL ARSLSTVAVR VVEVIPGKPY
     VGLELPNKKR QTVYLREVLD NAKFRDNPSP LTVVLGKDIA GDPVVADLAK MPHLLVAGTT
     GSGKSVGVNA MILSMLYKAQ PEDVRFIMID PKMLELSVYE GIPHLLTEVV TDMKDAANAL
     RWSVNEMERR YKLMSALGVR NLAGYNEKIA EAARMGRPIP DPYWKPGDSM DVQHPVLEKL
     PYIVVLVDEF ADLMMTVGKK VEELIARLAQ KARAAGIHLV LATQRPSVDV ITGLIKANIP
     TRIAFTVSSK IDSRTILDQG GAESLLGMGD MLFSGPNSTM PVRVHGAFVR DQEVHAVVQD
     WKARGRPQYV DGITSDSESE GGGSFDGGEE LDPLFDQAVN FVTQKRKASI SGVQRQFRIG
     YNRAARIIEQ MEAQGIVSAQ GHNGNREVLA PPPFE
//
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