ID   CYDD_BACSU              Reviewed;         575 AA.
AC   P94367;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=ATP-binding/permease protein CydD;
GN   Name=cydD; Synonyms=yxkN; OrderedLocusNames=BSU38730;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / BGSC1A1;
RX   PubMed=8969509; DOI=10.1099/13500872-142-11-3113;
RA   Yoshida K., Shindo K., Sano H., Seki S., Fujimura M., Yanai N., Miwa Y.,
RA   Fujita Y.;
RT   "Sequencing of a 65 kb region of the Bacillus subtilis genome containing
RT   the lic and cel loci, and creation of a 177 kb contig covering the gnt-
RT   sacXY region.";
RL   Microbiology 142:3113-3123(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
CC   -!- FUNCTION: Somehow involved in the cytochrome D branch of aerobic
CC       respiration. Seems to be a component of a transport system (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Cysteine
CC       exporter (TC 3.A.1.129.1) family. {ECO:0000305}.
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DR   EMBL; D83026; BAA11730.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15899.1; -; Genomic_DNA.
DR   PIR; D69611; D69611.
DR   RefSeq; NP_391752.1; NC_000964.3.
DR   RefSeq; WP_003244401.1; NZ_JNCM01000034.1.
DR   AlphaFoldDB; P94367; -.
DR   SMR; P94367; -.
DR   STRING; 224308.BSU38730; -.
DR   PaxDb; P94367; -.
DR   PRIDE; P94367; -.
DR   EnsemblBacteria; CAB15899; CAB15899; BSU_38730.
DR   GeneID; 936330; -.
DR   KEGG; bsu:BSU38730; -.
DR   PATRIC; fig|224308.179.peg.4192; -.
DR   eggNOG; COG4987; Bacteria.
DR   InParanoid; P94367; -.
DR   OMA; VSHNATF; -.
DR   PhylomeDB; P94367; -.
DR   BioCyc; BSUB:BSU38730-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0034775; P:glutathione transmembrane transport; IEA:InterPro.
DR   Gene3D; 1.20.1560.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR014223; ABC_CydC.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF90123; SSF90123; 1.
DR   TIGRFAMs; TIGR02868; CydC; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..575
FT                   /note="ATP-binding/permease protein CydD"
FT                   /id="PRO_0000092243"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        246..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          18..303
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          337..570
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         370..377
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   575 AA;  64510 MW;  FF17B481DF22A0BF CRC64;
     MKKEEWILPY IKQNARLFVL VIFLGAVTIF SAAFLMFTSG FLISKAATRP ENILLIYVPI
     VAVRTFGIAR SVSRYVERLV GHHIILKIVS DMRVRLYNML EPGALMLRSR FRTGDMLGIL
     SEDIEHLQDA FLKTIFPAIS ALLLYAVSVI ALGFFSWPFA ILLALYLFVL VVLFPVVSLL
     VTRAKNAKLK SGRNVLYSRL TDAVMGVSDW MFSGRRHAFI DAYEKEERDW FELERKKQRF
     TRWRDFAAQC LVAGLILLML FWTAGQQADG ELAKTMIAAF VLVVFPLTEA FLPLSDALGE
     VPGYQDSIRR MNNVAPQPEA SQTESGDQIL DLQDVTLAFR DVTFSYDNSS QVLHNFSFTL
     RQGEKMALLG RSGSGKSTSL ALIEGALKPD SGSVTLNGVE TALLKDQIAD AVAVLNQKPH
     LFDTSILNNI RLGNGEASDE DVRRAAKQVK LHDYIESLPD GYHTSVQETG IRFSGGERQR
     IALARILLQD TPIIILDEPT VGLDPITERE LMETVFEVLK GKTILWITHH LAGVEAADKI
     VFLENGKTEM EGTHEELLAA NERYRRLYHL DVPVK