ID Q4L785_STAHJ Unreviewed; 1297 AA.
AC Q4L785;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=FtsK domain-containing protein {ECO:0000259|PROSITE:PS50901};
GN OrderedLocusNames=SH1181 {ECO:0000313|EMBL:BAE04490.1};
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808 {ECO:0000313|EMBL:BAE04490.1, ECO:0000313|Proteomes:UP000000543};
RN [1] {ECO:0000313|EMBL:BAE04490.1, ECO:0000313|Proteomes:UP000000543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435 {ECO:0000313|EMBL:BAE04490.1,
RC ECO:0000313|Proteomes:UP000000543};
RX PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
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DR EMBL; AP006716; BAE04490.1; -; Genomic_DNA.
DR RefSeq; WP_011275482.1; NC_007168.1.
DR KEGG; sha:SH1181; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_12_5_9; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000000543; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; 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; 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:SF42; DNA TRANSLOCASE SFTA; 1.
DR PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 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}; Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}.
FT DOMAIN 971..1159
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 320..351
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 9..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..621
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..774
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 988..995
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1297 AA; 148145 MW; 9F095034659F58B4 CRC64;
MSWFDDLFSN KENSDEELLR RKSKRRNGDL TQNKDDSLLP ENNDIYDRPR GKFRFPIDVG
QDENYEEAIY RDSNDDIGSY RPHSSNDHSS YDSFDYDGHT NQSNNYAKYD SSEDSRRRRR
RNHINQDDTG IPSIKSRSPK SSNKYIDTRE SQRFNKHQNN YSSTNVSNYS KANSNHQSRV
KLQSERFKSN YHLSSEPTYH RSSFKTSEVP SAIFGTKKRR PIENGVIPPV KDDEDSKESI
TKYSSSTVEH VPHESNHAIA DNSNKEDTKR SSQLDSSITI ENESTIESSS NTSNNNERTP
NYSKRDNTVN IENIYASQIV EEIRKERERK VQQKRKFKEA LQNKRQQTDE EDSIQRAIDE
MYAKQAEQYT GESSLNQGDN VSNKSNESEI DKSKHSYHSK DKSLVDEHNG LVQNQTDEQT
NSDNVDNQTE VSNESHEPYN YEEIDLNQVS SVQQVRQDDV QVKDVLEEQS SKINNNKVES
YSNEKFDDYL EDTNSHEEML HDDDLHEQVM DDDENEGISN KTTDENNDEK IDDANYREIN
ESESLMQDKA NDLKFNDEVN NSENQQNSSE NNINNAVRNA VSSDIEYATN EDEENDERLA
QDTNKEDQKL SQSEDIQHES LNNEDVSLTS NKTDDSEHLE KDSLNEDKKA EPSFNKTNKA
PQKMSIKPGS KPFNVVMTPS DKKRVMDAKK NSVSRNKVNV PELKPETKKE AQDEKMNAEF
DNHLNESQLN SDESSDFNVA SLEYNESSEH SVEKDNIIND ENTRENEHQD VDNSQNNDMP
KGNQFSKVQN SNNQNDNKHD INEFVSKEGY SEVTSTKNHK DGDDANHKAP IRRGPNIKLP
SLDLLEDHEE HEIDESWIEE KKQELNDAFY YFNVPAEVQN VTEGPSVTRF ELAVEKGVKV
SRITALQDDI KMALAAKDIR IEAPIPGTSL VGIEVPNLNP TKVNLKSILE SPKFKNAESK
LTVAMGNRIN NEPLLMDIAK TPHALIAGAT GSGKSVCINS ILMSLLYKNH PEELRLLLID
PKMVELAPYN DLPHLVSPVI TDVKAATQSL KWAVDEMEKR YKLFAQFHVR NITAFNKKAP
YEQRMPKIVI VIDELADLMM MAPQEVEQSI ARIAQKARAC GIHMLVATQR PSVNVITGLI
KANIPTRIAF MVSSSVDSRT ILDSGGAERL LGYGDMLYLG SGMNKPIRVQ GTFVSDDEID
DVVDFIKDQR EPDYLFEEKE LLKKNQTQAQ DELFDDVCEF MVKEGHISTS LIQRHFQIGY
NRAARIVDQL EQLDYISGAN GSKPRDVFIT EADLKKE
//
