MOTB_HELPY
ID MOTB_HELPY Reviewed; 257 AA.
AC P56427;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Motility protein B;
DE AltName: Full=Chemotaxis protein MotB;
GN Name=motB; OrderedLocusNames=HP_0816;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
CC -!- FUNCTION: MotA and MotB comprise the stator element of the flagellar
CC motor complex. Required for the rotation of the flagellar motor. Might
CC be a linker that fastens the torque-generating machinery to the cell
CC wall (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Each stator complex is composed of 4 MotA and 2 MotB subunits.
CC 2 A subunits and 1 B subunit are thought to form a single ion channel,
CC so that each stator complex contains two channels (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P56427; P56427: motB; NbExp=3; IntAct=EBI-7611014, EBI-7611014;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass
CC type II membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MotB family. {ECO:0000305}.
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DR EMBL; AE000511; AAD07865.1; -; Genomic_DNA.
DR PIR; H64621; H64621.
DR RefSeq; NP_207609.1; NC_000915.1.
DR RefSeq; WP_001085308.1; NC_000915.1.
DR PDB; 3CYP; X-ray; 1.60 A; B/C/D/E=126-257.
DR PDB; 3CYQ; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=126-257.
DR PDB; 3IMP; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=126-257.
DR PDB; 3S02; X-ray; 2.50 A; A/B=104-257.
DR PDB; 3S03; X-ray; 2.50 A; A/B/C/D=98-257.
DR PDB; 3S06; X-ray; 1.80 A; A/B=98-257.
DR PDB; 3S0H; X-ray; 2.10 A; A/B/C/D=91-257.
DR PDB; 3S0W; X-ray; 2.50 A; A/B=79-257.
DR PDB; 3S0Y; X-ray; 1.80 A; A/B=65-257.
DR PDBsum; 3CYP; -.
DR PDBsum; 3CYQ; -.
DR PDBsum; 3IMP; -.
DR PDBsum; 3S02; -.
DR PDBsum; 3S03; -.
DR PDBsum; 3S06; -.
DR PDBsum; 3S0H; -.
DR PDBsum; 3S0W; -.
DR PDBsum; 3S0Y; -.
DR AlphaFoldDB; P56427; -.
DR SMR; P56427; -.
DR DIP; DIP-3662N; -.
DR IntAct; P56427; 4.
DR MINT; P56427; -.
DR STRING; 85962.C694_04180; -.
DR PaxDb; P56427; -.
DR EnsemblBacteria; AAD07865; AAD07865; HP_0816.
DR KEGG; hpy:HP_0816; -.
DR PATRIC; fig|85962.8.peg.848; -.
DR eggNOG; COG1360; Bacteria.
DR OMA; NWHLSSA; -.
DR PhylomeDB; P56427; -.
DR EvolutionaryTrace; P56427; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0097588; P:archaeal or bacterial-type flagellum-dependent cell motility; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR CDD; cd07185; OmpA_C-like; 1.
DR Gene3D; 3.30.1330.60; -; 1.
DR InterPro; IPR025713; MotB_N_dom.
DR InterPro; IPR006665; OmpA-like.
DR InterPro; IPR036737; OmpA-like_sf.
DR Pfam; PF13677; MotB_plug; 1.
DR Pfam; PF00691; OmpA; 1.
DR SUPFAM; SSF103088; SSF103088; 1.
DR PROSITE; PS51123; OMPA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Chemotaxis;
KW Flagellar rotation; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..257
FT /note="Motility protein B"
FT /id="PRO_0000189588"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..257
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 113..236
FT /note="OmpA-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00473"
FT REGION 74..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 77..83
FT /evidence="ECO:0007829|PDB:3S0Y"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:3S0Y"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:3S0Y"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:3S06"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:3S06"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:3S06"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3S0Y"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:3S06"
FT HELIX 136..149
FT /evidence="ECO:0007829|PDB:3CYP"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:3CYP"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:3CYP"
FT HELIX 177..194
FT /evidence="ECO:0007829|PDB:3CYP"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:3CYP"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:3CYP"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:3S0H"
FT HELIX 219..225
FT /evidence="ECO:0007829|PDB:3CYP"
FT STRAND 226..235
FT /evidence="ECO:0007829|PDB:3CYP"
FT HELIX 236..250
FT /evidence="ECO:0007829|PDB:3CYP"
SQ SEQUENCE 257 AA; 28849 MW; 58C1774B0547C032 CRC64;
MAKKNKPTEC PAGEKWAVPY ADFLSLLLAL FIALYAISAV NKSKVEALKT EFIKIFNYAP
KPEAMQPVVV IPPDSGKEEE QMASESSKPA SQNTETKATI ARKGEGSVLE QIDQGSILKL
PSNLLFENAT SDAINQDMML YIERIAKIIQ KLPKRVHINV RGFTDDTPLV KTRFKSHYEL
AANRAYRVMK VLIQYGVNPN QLSFSSYGST NPIAPNDSLE NRMKNNRVEI FFSTDANDLS
KIHSILDNEF NPHKQQE
