ID A0A221MEM9_9BACI Unreviewed; 1476 AA.
AC A0A221MEM9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Type VII secretion protein EssC {ECO:0000313|EMBL:ASN06084.1};
GN Name=essC {ECO:0000313|EMBL:ASN06084.1};
GN ORFNames=CFK40_14185 {ECO:0000313|EMBL:ASN06084.1};
OS Virgibacillus necropolis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=163877 {ECO:0000313|EMBL:ASN06084.1, ECO:0000313|Proteomes:UP000204391};
RN [1] {ECO:0000313|EMBL:ASN06084.1, ECO:0000313|Proteomes:UP000204391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 19488 {ECO:0000313|EMBL:ASN06084.1,
RC ECO:0000313|Proteomes:UP000204391};
RX PubMed=12710619; DOI=10.1099/ijs.0.02371-0;
RA Heyrman J., Logan N.A., Busse H.J., Balcaen A., Lebbe L.,
RA Rodriguez-Diaz M., Swings J., De Vos P.;
RT "Virgibacillus carmonensis sp. nov., Virgibacillus necropolis sp. nov. and
RT Virgibacillus picturae sp. nov., three novel species isolated from
RT deteriorated mural paintings, transfer of the species of the genus
RT salibacillus to Virgibacillus, as Virgibacillus marismortui comb. nov. and
RT Virgibacillus salexigens comb. nov., and emended description of the genus
RT Virgibacillus.";
RL Int. J. Syst. Evol. Microbiol. 53:501-511(2003).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP022437; ASN06084.1; -; Genomic_DNA.
DR KEGG; vne:CFK40_14185; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000204391; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR023839; Firmicutes_EssC_C.
DR InterPro; IPR022206; Firmicutes_EssC_N.
DR InterPro; IPR002543; FtsK_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR03928; T7_EssCb_Firm; 1.
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; PF12538; FtsK_SpoIIIE_N; 1.
DR SMART; SM00382; AAA; 3.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR PROSITE; PS50901; FTSK; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000204391};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 227..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 643..839
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT DOMAIN 972..1158
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT BINDING 663..670
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT BINDING 991..998
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1476 AA; 169909 MW; FD7991167DF74B8D CRC64;
MKHLWLFYDQ VYHYVELPDE QTDVISIGND IHHIITVQLF TIEPSLTVEI QNDQLVVYQD
GNFQGEIGYQ SPLTLTIDGH KMTFAMREGN LIEKTFYIGN QQEVNVDDET KTLHYLLFRN
EKQWFVKPYQ DDIYINGHKI DSITPIVLGD SVFHPYSFMT MTKNDSITIA STSTIPLSLP
VIKEPTTDLK QKYPVYRRTP RMVYDLPDDK ISFSFPSEEG EDNRRGLMLI IMPPLVMLLV
MGMVTLVQPR GIFILISVSM FATTLVTSTI QFFKEKKLQR EKKKKRIRLY TRYLENKRDE
LQKLAVKQRD ILYYHFPSFE KMKYLTAEVS NRIWERTMMS RDFLHYRIGR ATVPSSYNVS
VQSGDMSNQE IDDLLEKSQE LVAHYKYVKN VPLTIDLSTG PTGLVGKDSI VKSEIQQIVG
QLSFSQSYHD VRFVAIFDEE EYEYWEWMKW LPHFQLPHAY AKGFIYNEQT RDQLLSSIYE
ILKERDLDNE KDKKMFVPHL IFIVTNRQLI SEHVILEYLE GNHTDIGIST IFAADTKESL
SENIHTLVRY INEQEGDILI QQQKAIHTPF WLDEHTQADN EKFSRMLRSM NHQLGMSNSI
PDKVSFMGLM QVDKAEELQI SEKWLKNQSS KTLAVPIGLK GKDDQVFLNL HEKAHGPHGL
LAGTTGSGKS EFLQTYILSL AVHFHPHEVA FLLIDYKGGG MAQPFKFIPH LLGTITNIEG
NKNFSKRALA SIKSELKRRQ RLFDTYEVSH ISDYTALYKS NEAKEPLPHL FLISDEFAEL
KNEEPEFIRE LVSAARIGRS LGVHLILATQ KPGGIIDDQI WSNARFKVAL KVQDDSDSKE
ILKNPDAAKL SVTGRGYLQV GNNEVYELFQ SAWSGAPYAK DAFGTEDDVA LVTDLGLVPL
SDVSAEEGSK KNKITEIEMI TKEIAQVQEN MDIHKLPSPW LPPLPERLSY SSEVPSDTEG
YYIGMIDEPE MQRQTNYSYQ PMDDGNIGIF GSSGYGKSTT VLTLLLNFAR KNSPDSFQYY
IFDFGNGALL PLQQLPHTGD YFRSDDQRKI EKFLVFINDD MERRKQLFRD QEVSNIKMYN
MVSEQPLPLL FITLDNFDLV KEEMQDLENK FTQIARDGQS LGIYTILTAT RTNAVRQALM
SNLKTKIVHY LMDAGEKFTV LGRTQYETEA VQGRAYIQKE ESYLAQLFLP TEGENDVEML
ENVKQVVQYL KDIYQEAEKP KEIPMLPRKL DFVAFRKSYE MDKVKKLIPI GLDEDSVKPT
YMDFQKDKHC LIVGDVQKGK TNILKLILHT MKDSKDNKIA VFDSVNHGLA EYADDEQVVY
METKEQVEGW LQIADAEFLK REEEYRDALN TRKTASLGFE PFILLIDGMD NFRGNIDSLI
QSKLANYIKN YSHLGFSIIV TGNTGEFTKG FDPFTNEVKL IKQAILLMRK TDQSMFNLPY
TRNEAEIQAG FGYHINSGRV RKIQIPLCES ERMTSV
//
