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Database: UniProt
Entry: K8WWP4_9GAMM
LinkDB: K8WWP4_9GAMM
Original site: K8WWP4_9GAMM 
ID   K8WWP4_9GAMM            Unreviewed;       702 AA.
AC   K8WWP4;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Alpha-hemolysin translocation ATP-binding protein HlyB {ECO:0000256|ARBA:ARBA00015531};
GN   ORFNames=OOA_09418 {ECO:0000313|EMBL:EKT61812.1};
OS   Providencia burhodogranariea DSM 19968.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Providencia.
OX   NCBI_TaxID=1141662 {ECO:0000313|EMBL:EKT61812.1, ECO:0000313|Proteomes:UP000009336};
RN   [1] {ECO:0000313|EMBL:EKT61812.1, ECO:0000313|Proteomes:UP000009336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19968 {ECO:0000313|EMBL:EKT61812.1,
RC   ECO:0000313|Proteomes:UP000009336};
RX   PubMed=23145767; DOI=10.1186/1471-2164-13-612;
RA   Galac M.R., Lazzaro B.P.;
RT   "Comparative genomics of bacteria in the genus Providencia isolated from
RT   wild Drosophila melanogaster.";
RL   BMC Genomics 13:612-612(2012).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Protein-1
CC       exporter (TC 3.A.1.109) family. {ECO:0000256|ARBA:ARBA00006025}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKT61812.1}.
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DR   EMBL; AKKL01000023; EKT61812.1; -; Genomic_DNA.
DR   RefSeq; WP_008911899.1; NZ_KB233222.1.
DR   AlphaFoldDB; K8WWP4; -.
DR   STRING; 1141662.OOA_09418; -.
DR   PATRIC; fig|1141662.3.peg.1910; -.
DR   eggNOG; COG2274; Bacteria.
DR   HOGENOM; CLU_000604_95_4_6; -.
DR   OrthoDB; 6828292at2; -.
DR   Proteomes; UP000009336; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030256; C:type I protein secretion system complex; IEA:InterPro.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR   GO; GO:0030253; P:protein secretion by the type I secretion system; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd18588; ABC_6TM_CyaB_HlyB_like; 1.
DR   Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR010132; ATPase_T1SS_HlyB.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005074; Peptidase_C39.
DR   InterPro; IPR039421; Type_1_exporter.
DR   NCBIfam; TIGR01846; type_I_sec_HlyB; 1.
DR   PANTHER; PTHR24221:SF662; ALPHA-HEMOLYSIN TRANSLOCATION ATP-BINDING PROTEIN HLYB; 1.
DR   PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF03412; Peptidase_C39; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS50990; PEPTIDASE_C39; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        152..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        259..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        287..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..121
FT                   /note="Peptidase C39"
FT                   /evidence="ECO:0000259|PROSITE:PS50990"
FT   DOMAIN          152..431
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          464..699
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   702 AA;  79066 MW;  BB20BE5D0F0E8686 CRC64;
     MATNQNNYGL EALVWIANYY QKNVTKDQLM HSIGMQSISP TDWEIRECAH ISGYETSLLA
     LDKPILTDIP LPALICLNGY WLVLSKNKDD EHILIHPETG EQSKWCNYKL NETANISLLL
     VKEQFESEQK IKFGIGWFIP SILRQRSQLK NIFILAAIVQ LFALISPLLF QNVIDKVLVG
     RSLNSLHVLA IAIVSISFAE PIYSFIRNKI FSHTSTQISA ELSGKLYRHL MALPLNYFKL
     RPTGKIIARI REMAHIRQFL TGSTLMLFID LLFVSLFIAV LFSYSAIMSW ILIGSLVVFF
     ILWMILGPII RQQTEKSYQA DENGLTFLTE AITGIETIKT TATEKYFYQR WQKLLSKQLT
     QGFKVSIRSE VASQLMTLVS KITIAALLWV GVKEVMNGGI TPGELVAYNM LSAHVTQPVL
     RLAQIWQDFQ HTIISLRRVG DILDEPVENE RKGIVSSASI QGQIDFQNIR FRYQPETPEV
     LNNLSLSVKA GEFIGITGPS GSGKSTLTKL LQRLYIPQHG QVIVDGMDLS VSDTVALRRR
     MSVVLQESML FVGTIKENIR LSKPQASDHD IIQSAKLAGA YEFVMSLPDN FDYHLSERGL
     NLSGGQRQRI ALARALLTEP DILILDEATS ALDYESEAAI MANMPLITKG RTVISIAHRL
     NTIMHADKIC VIRDGEVAEM DTHENLLQQN GVYAHLWQQQ TS
//
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