ID A0A127A045_9MICC Unreviewed; 1508 AA.
AC A0A127A045;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Protein EssC {ECO:0000313|EMBL:AMM32231.1};
GN ORFNames=SA2016_1554 {ECO:0000313|EMBL:AMM32231.1};
OS Sinomonas atrocyanea.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Sinomonas.
OX NCBI_TaxID=37927 {ECO:0000313|EMBL:AMM32231.1, ECO:0000313|Proteomes:UP000070134};
RN [1] {ECO:0000313|EMBL:AMM32231.1, ECO:0000313|Proteomes:UP000070134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 3377 {ECO:0000313|EMBL:AMM32231.1,
RC ECO:0000313|Proteomes:UP000070134};
RA Kim K.M.;
RT "Complete genome of Sinomonas atrocyanea KCTC 3377.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP014518; AMM32231.1; -; Genomic_DNA.
DR RefSeq; WP_066497079.1; NZ_CP014518.1.
DR STRING; 37927.SA2016_1554; -.
DR KEGG; satk:SA2016_1554; -.
DR PATRIC; fig|37927.3.peg.1602; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000070134; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR CDD; cd00060; FHA; 1.
DR CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR002543; FtsK_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR032030; YscD_cytoplasmic_dom.
DR PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
DR PANTHER; PTHR22683:SF1; TYPE VII SECRETION SYSTEM PROTEIN ESSC; 1.
DR Pfam; PF01580; FtsK_SpoIIIE; 2.
DR Pfam; PF16697; Yop-YscD_cpl; 1.
DR SMART; SM00382; AAA; 3.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS50901; FTSK; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000070134};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 265..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 150..198
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 709..897
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT DOMAIN 1035..1226
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 519..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 727..734
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT BINDING 1053..1060
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1508 AA; 160272 MW; E9102519D981B629 CRC64;
MRIRLTLRRD PEPAVDLAVT VDGLASVGDV ARELWLADPA RAAEHTGAGP ARAEAGALAG
LTLRVEESVL AGGMTGRVLD PEGTFLESGL RQGSTVSLSR VAPRGAAHGA AGADSGAGAP
AVDRGPAAAT LRVVSGPDAG REFSLPVGAS LIGRGAGADV VLTDPLVSKR HARITVGETI
EIADLNSSNG LVMDGLTVSK AVLASSDAVT LGDSTVSVVG LGHSAGRTQT SPLVPFNRSP
RVVPRFPPQA RELPEGPQRP TTQPFPIVML FVPILMGAVM FAVLQSVVSI VFMAMMPLFA
VGMWFEYRRH ARRELREETR LFEERLAEFA RQITELQTVE RAVRLQEAPS VAETVESIYR
LGPLLWTHAP EHREFLTVRL GLGTVPSRVS VTVPPEGRTL PEFTRRLHEA QGRFAVLDAV
PVTASLRQGG GLGVAGPRGL VENVARGILL QIAGLHSPAE VVIAGLASHE SKERWEWLQW
LPHVGSSHSP LAGDHLAAGS AAGMLLLTRL EDLLAVRTAG PDGQASPSGG PAGRRGAVRE
EHDGTSEPIV PTVVVLVEDD APVDRGRLTR IAELGPDVGI HVVWVAAGAE QLPQCCRDFI
VVDGEHGATS GQVRLGRHTY PVSCESVDEA LAVQLGRMLT PIVDVGKPVD DDSDLPRSVS
YVTLAGAEIA DDAGTVAERW QQSNSVRASA VANPKAKGTL RALVGSKGVE QFFLDLKNEG
PHALVGGTTG AGKSEFLQSW VLGMANAYSP DRVTFLFVDY KGGAAFADCV SLPHTVGLVT
DLSPHLVRRA LTSLRAELHY REHLFNRKKA KDLLAMERAA DPDTPPYLVI VVDEFAALAT
EVPEFVDGVV DVAARGRSLG LHLILATQRP AGVIKDSLRA NTNLRIALRM ADEADSEDIL
GEKTAAYFDP GIPGRGAAKT GPGRIQGFQT GYASGWTTER PALPRIDIAE MDFGTGAAWE
RPADLVDAEP EAEGPNDIAR MVRTISTAAD RIGLEMPRKP WLAELPQTYD VARLPNPRTD
ERLLLGVVDD PAHQSQPTFF YEPDRDGNMA VYGTGGSGKS AALRTVAVAA AITMRGGPVQ
VYGIDAGSRG LHMLEALPHV GAVIDADDAE RIGRLMRHLS GLVDERSERY AAARAGSIGE
YRRLAGRPDE PRIIVLIDGM GAFREQYEYS SESAVFDLLT QLASDGRAVG VHLVMTGDRT
NSIPASIASS VQKRIILRMT GEDDYMMFGQ PKDVVTPQSP PGRGVVDGLE VQLGVLGGNA
NVALQAREIT RLAEAMRRQG VPEAPPVRTL PDLVTGQALP TDSGRVALGL EDSTLEPLYV
DPSGAFMLTG PPGSGRTTAL AALAAGLRRA RPGVRRVYLG ARRSALANLP LWDASFTGED
AVAAAVDELQ LDVGVREFAL FVEGLPDFDS TLAESGLSGL ITAMDREGLW IVGESETAGW
GSAWSLSQPF KNGRRGLLLN PAEMDGDSLL NTSLGRIRNP RYVPGRGFYV ARGRAYKVQA
AFEDLAAG
//
