ID Q49YH2_STAS1 Unreviewed; 1250 AA.
AC Q49YH2;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE SubName: Full=Putative DNA segregation ATPase FtsK SpoIIIE family protein {ECO:0000313|EMBL:BAE18167.1};
GN OrderedLocusNames=SSP1022 {ECO:0000313|EMBL:BAE18167.1};
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451 {ECO:0000313|EMBL:BAE18167.1, ECO:0000313|Proteomes:UP000006371};
RN [1] {ECO:0000313|EMBL:BAE18167.1, ECO:0000313|Proteomes:UP000006371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41
RC {ECO:0000313|Proteomes:UP000006371};
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
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DR EMBL; AP008934; BAE18167.1; -; Genomic_DNA.
DR RefSeq; WP_011302869.1; NZ_MTGA01000033.1.
DR AlphaFoldDB; Q49YH2; -.
DR KEGG; ssp:SSP1022; -.
DR PATRIC; fig|342451.11.peg.1021; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_12_5_9; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000006371; 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 DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000006371}.
FT DOMAIN 924..1112
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 941..948
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1250 AA; 141847 MW; 76A21E618F9D5E3E CRC64;
MSWFDKLFGE DNESTDNYLN KRSQRRQKAT QKEEHDSLLP QNNDVYERPK GKFRFPMRVL
EEANDSLKTD DELNSDIAST SHKTSHDAHN DVSHGNAHHQ QRRRRHMYDK TPTQNINSSD
SVGQQSQQQD HYQTENETRT HKGKRMRIQT DVLRANASSK HKPTTSNFHH SDFKASEVPS
AIFGTKKPRP LENGVIKRQD DSEEGTQAEN ETNHRNYNDE SSQQKHQTVK DSDSNSTDIQ
NEAHMYHENS NDTAYDLSDN KERRDAQHVE ENGEEVELNQ PVTSQNKKDN TIKIENIYAS
QIVEEIRRER ERKVLQKRQF KKALQQKRHD NQDKQEDSIQ KAIDEMYAKQ ARNYIGESSL
DEDGNAMNMS KSKTSTSRQS AENQQQTEST NSEDIEEDSN TPFNYEEVDL DHVRDVHTIN
NEQVNVNTKN DSSAIEADQN QVEQVTPNSD FENQNDENNT AIESSQSDMS ENERTYILEK
SFERYLDEND VDDAQYRELS ETDPKSKESL AFDSLDSQSE NEQLSESLSQ PDHGFENSES
DIIDNHVTSN DAAPSEASQL ESDESMNENE SLNVQNEILD ERSELEQSDS TDNNNGNHIK
QPDETKTYKK ATSIKKGSKP FNVVMTPSDK KRMLDAQKEK NKSNIQLNNV DNFKHNTSSD
ISDKQSQSNN DQLANEPASE SLTVTDDNQS ETNLSHDLID EQSDFKPETD ASFYSDDYNR
NDSTQSNVQQ ESVESAESDM TNVPSEQNEN HKQNVQEPVL KPETSGNQLG GVNTSTEDDN
KATIRRGPNI KLPSIELLEA PKQHEIDNAW IEDKKQELNE AFYYFNVPAE VQNVTEGPSV
TRFELSVEKG VKVSRITALQ DDIKMALAAK DIRIEAPIPG TSLVGIEVPN QNATTVNLRS
ILEKPAFKNA ESKLTVAMGL RINNEPLLMD ISKTPHALIA GATGSGKSVC INSILMSLLY
KNHPEELRLL LIDPKMVELA PYNDLPHLVA PVITDVKAAT QSLKWAVEEM ERRYKVFAKY
HVRNITAFNK KATYEDRMPK IVIVIDELAD LMMMAPQEVE QSIARIAQKA RACGIHMLVA
TQRPSVNVIT GLIKANIPTR IAFMVSSSVD SRTILDSGGA ERLLGYGDML YLGSGMNKPI
RVQGTFVSDE EIDDVVDFIK QQRDPEYLFE EKELLKKTES QPQDDLFDDV CRFMLNEGHI
STSLVQRHFQ IGYNRAARII DQLEQLGYVS GANGSKPRDV YITESDLNEN
//
