MBAA_VIBCH
ID MBAA_VIBCH Reviewed; 791 AA.
AC Q9KU26;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Biofilm architecture maintenance protein MbaA;
DE Flags: Precursor;
GN Name=mbaA; OrderedLocusNames=VC_0703;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP FUNCTION.
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=12562809; DOI=10.1128/jb.185.4.1384-1390.2003;
RA Bomchil N., Watnick P., Kolter R.;
RT "Identification and characterization of a Vibrio cholerae gene, mbaA,
RT involved in maintenance of biofilm architecture.";
RL J. Bacteriol. 185:1384-1390(2003).
RN [3]
RP FUNCTION.
RC STRAIN=MO10 / Serotype O139;
RX PubMed=16237027; DOI=10.1128/jb.187.21.7434-7443.2005;
RA Karatan E., Duncan T.R., Watnick P.I.;
RT "NspS, a predicted polyamine sensor, mediates activation of Vibrio cholerae
RT biofilm formation by norspermidine.";
RL J. Bacteriol. 187:7434-7443(2005).
CC -!- FUNCTION: Plays an essential role in the maintenance and the formation
CC of the three-dimensional structure of the biofilms at the later stages
CC of their development. Absence of mbaA promotes the accumulation of
CC larger amount of biomass on the surfaces at later stage of development,
CC results in the overproduction of an extracellular polymeric substance
CC that accumulates in the matrix of biofilms. This yields biofilms
CC lacking the typical structure consisting of pillars of cells separated
CC by fluid filled channels. {ECO:0000269|PubMed:12562809,
CC ECO:0000269|PubMed:16237027}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC type I membrane protein {ECO:0000305}.
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DR EMBL; AE003852; AAF93868.1; -; Genomic_DNA.
DR PIR; A82291; A82291.
DR RefSeq; NP_230352.1; NC_002505.1.
DR RefSeq; WP_000773112.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KU26; -.
DR SMR; Q9KU26; -.
DR STRING; 243277.VC_0703; -.
DR DNASU; 2615707; -.
DR EnsemblBacteria; AAF93868; AAF93868; VC_0703.
DR GeneID; 57739416; -.
DR KEGG; vch:VC_0703; -.
DR PATRIC; fig|243277.26.peg.673; -.
DR eggNOG; COG5001; Bacteria.
DR HOGENOM; CLU_000445_70_45_6; -.
DR OMA; QFRQANI; -.
DR BioCyc; VCHO:VC0703-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
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:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd01948; EAL; 1.
DR CDD; cd01949; GGDEF; 1.
DR Gene3D; 3.20.20.450; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR Pfam; PF00563; EAL; 1.
DR Pfam; PF00990; GGDEF; 1.
DR SMART; SM00052; EAL; 1.
DR SMART; SM00267; GGDEF; 1.
DR SUPFAM; SSF141868; SSF141868; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR TIGRFAMs; TIGR00254; GGDEF; 1.
DR PROSITE; PS50883; EAL; 1.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..791
FT /note="Biofilm architecture maintenance protein MbaA"
FT /id="PRO_0000042814"
FT TOPO_DOM 24..259
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..791
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 281..333
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 368..509
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT DOMAIN 518..769
FT /note="EAL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00074"
SQ SEQUENCE 791 AA; 90794 MW; 2AC4CCFF8CE84623 CRC64;
MKLNHRILLL IAPVILLSAA ASSYIIYTSQ KNALLKRTDS YLQLNIEKLA SHYRQAQSLV
SSYAFTLAKS DIIRHYFSLE KNPYRELELV DNLRETLQIL QPNEKQLVSL SILNGHEELL
YYAENSSDPF AELDPKVMAY IKQRFASTQK NSDISYTVNS AGEDILVRYD MLDTQTLSTP
LSYNRQDVFF VVVYVVLEQF SQLRKKIEFD NQSPIFFTHS PPSYRTGLLQ SVELQPGFYA
ILDPAPKLIN AQLHSIQREL LLSFGVSALV TVLMLLLLLY RHVINPILHL DKQLEEVENN
QRKNIEKLNT DDEIGRLSSR FYAMYSELHS TYQRTKALAE NDHLTKLANR YQFQVQADLL
LSRCYDTQHI WVMYIDLDNF KYVNDKYGHQ IGDSLLVSFA THVRQLCKNF EASHNTYSIA
ARLSGDEFAI LLVSPKRFND CAKIFAQRLL APIQNKDNSP LSHFPITASI GIATFPKDGE
HIEKLLLNAD TAMYQAKNAG KNQVAYYSQA LDQIVQRRNN IERALRLGLF DQEFNLAYQP
YFTCSGKRLV GFEVLLRWQS ELLGEVSPEE FIPIAEQTGL FGTIDRWVIS KAFQEISTLQ
AIVKEPIQVS INLSSAELNS LKLAQFIHRQ AEQFGVSPAW IDFEITETFA ADSQSFPLLH
ELSRLGYGLT IDDFGSGYTS ITQLVQYPVQ KIKFDRHFLD TLIATNKQNV IRPLIDLCHS
QSMKVTAEGI ESETMHQWLA DYECDYMQGF YFGYPMSLSE ISPWLHASNH KKKSYAQDHY
CFTEPSQSEC R
