HMW1_MYCGA
ID HMW1_MYCGA Reviewed; 1969 AA.
AC Q7NAT4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Cytadherence high molecular weight protein 1;
DE AltName: Full=Cytadherence accessory protein 1;
GN Name=hlp1; Synonyms=hmw3; OrderedLocusNames=MYCGA5510; ORFNames=MGA_0306;
OS Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS (Mycoplasmoides gallisepticum).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=710127;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R(low / passage 15 / clone 2);
RX PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT "The complete genome sequence of the avian pathogen Mycoplasma
RT gallisepticum strain R(low).";
RL Microbiology 149:2307-2316(2003).
CC -!- FUNCTION: Component of the cytoskeleton-like structure which stabilizes
CC the shape of the wall-less Mycoplasma. This cytoskeleton-like network
CC of accessory proteins containing HMW proteins 1 to 5 allows the proper
CC anchoring of cytadhesin proteins in the mycoplasmal membrane at the
CC attachment organelle (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell projection, attachment organelle membrane
CC {ECO:0000250}. Note=Localizes specifically to the attachment membrane.
CC {ECO:0000250}.
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DR EMBL; AE015450; AAP56901.2; -; Genomic_DNA.
DR RefSeq; WP_011113808.1; NC_004829.2.
DR AlphaFoldDB; Q7NAT4; -.
DR SMR; Q7NAT4; -.
DR KEGG; mga:MGA_0306; -.
DR PATRIC; fig|233150.7.peg.623; -.
DR HOGENOM; CLU_235452_0_0_14; -.
DR OrthoDB; 2038359at2; -.
DR Proteomes; UP000001418; Chromosome.
DR GO; GO:0033111; C:attachment organelle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0020035; P:adhesion of symbiont to microvasculature; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.3600; -; 7.
DR InterPro; IPR021199; Cytadherence_HMW-1_N.
DR InterPro; IPR022466; EAGR_box.
DR InterPro; IPR038145; EAGR_sf.
DR Pfam; PF16713; EAGR_box; 7.
DR TIGRFAMs; TIGR03834; EAGR_box; 7.
DR TIGRFAMs; TIGR03836; termin_org_HMW1; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cell projection; Coiled coil; Cytadherence; Membrane;
KW Reference proteome; Repeat; Virulence.
FT CHAIN 1..1969
FT /note="Cytadherence high molecular weight protein 1"
FT /id="PRO_0000380119"
FT REPEAT 148..166
FT /note="HAT 1"
FT REPEAT 258..278
FT /note="HAT 2"
FT REPEAT 300..331
FT /note="HAT 3"
FT REPEAT 333..353
FT /note="HAT 4"
FT REPEAT 477..497
FT /note="HAT 5"
FT REPEAT 959..997
FT /note="HAT 6"
FT REPEAT 1029..1067
FT /note="HAT 7"
FT REGION 174..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1000..1027
FT /evidence="ECO:0000255"
FT COILED 1082..1190
FT /evidence="ECO:0000255"
FT COILED 1547..1621
FT /evidence="ECO:0000255"
FT COILED 1758..1790
FT /evidence="ECO:0000255"
FT COMPBIAS 176..241
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..390
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1969 AA; 227910 MW; D7418FDEA5FCE98F CRC64;
MPKMIKGTEF IVAKKTKNKK KNHFEDIQTT NDINEEESEA IFGNLYDGAD EVLPASLAYE
NGQLPEDGSI QVAFDADDNA YYISYDPENE IFIEPYEKYE LDVSALYDAE GNPFDFFANY
HVEGAETSQE EESGEYWEQF VGVEGYGYYD ENEEWVWTGY FDEDNKFIPN EEEKPAEVEA
LEEESEATEE VVEQEPQEEV QAEEVVEEPV SQEQPEEEVA AEEYAEAAQE EYEEQPESEQ
EGSGEYWEQF VGVEGYGYYD ENNDWVWTGY FDENNNFVPD QYYDEDAAVA GDEQVEEYSA
QQEQVQEEYE QQPEQEGSGE YWEQFVGVEG YGYYDENNDW VWTGYFDENN NFVPDQYYDE
YAQPVSEEQY SESVSEEQEP ASEEQVAEEP AQVEEVAVEQ VPEETQPEQV QEKVQAYEHV
EEQQPEEVFA DAIDEHYDEI THVEDKAVEE EQIQTDNVVS SDEINWSNYV GNEDYGYYDE
NNEWVWKGYF NEYGMFIPQE EDYTDSIPVD EQPVEQTADL AEQNEEEVIE ETTASDEIVQ
VEEEVESEPV VPTVSDDLVA LEQPFEFDTQ QFVGNIDFGY YDESSEWIWT GHFDKDGKFF
DFDGNLVYSP QEGVKPVEVP KPTDLTNQIP QNALVVAEPD VFSEDTIQQV DESQFDVGEE
LVVRGLLNPA STPVQPQELN IKPVFEEEKL NLPVLANEVS LQPQVDYSKR SDFDQLVTQT
PVVLEDVVAD DLISVDTKGF VPELSQPTFA PKAVSQDQFK LVQPVVSQPK FDQITHLTDE
IKMDVNVTSS DVDVQPIQIN PSLEVASEPS KLDIFVKKPA VELKKIEFIE PVSEKIDLQI
FEQQEIVTKP VSTIQKPTYT DETVSVSVNA IDETTSETDT IVQVTPTTSE ASDFDINKIL
NTKPVETITV ELPKDEPKLV TGVHVSLVDV EAKPVEEIVK FDSPKPSVSE VVVEKEDKLT
LVEEEPFFNK FIGNEQYGYY NNKNVWIWTG YFDDQNNFVS DKDSKTQKVD QLIEEFNKQE
AIKKTEEVEA KKASEPFYNK YIGNKQFGYY NDKNVWIWNG YFDENDQFVP DQSWTKRSEK
LIEDELQKQR IHELELELAQ AQQAILESTK LKDQEVAKIK EEVLKVQQEA IKAKEVATLR
NFVPKGSPLL NPAKEVENSM IVYQEDKLEV NDLRNELSKL KTQREEFDNF SKIRDLDVIN
LYNASTSHRG MDYVFSGFEK KEEQFVKKPL HFLEEVKADP VQVAKEETIS NLDQLLKQDP
HLLLAKKTDK SVSPQASLTV LADQKEVELT QQAVRKQAEA IEAERVDVIK PLEQVQLNQS
RSLLDDLTPK FEVKPSLIKD DVIQPKYNDD LEPIEQLQFK QERSLLDDYM PKFDDQGLFS
KVEFKLPTVN KEYRPKVEPI DVIKPLEPVR INKERSLLDD YLPPKLNAQP TFEKTELDLG
LEKPLANGEL YEELKAEFST TITPADSKDM IDQLLEETND LITSSTQTRS TKIHSFSKSP
LKTEPEPILD TKFDDKFIEL DENQGFDQLI VESDDELLTD VVQEQVSVNQ IAVTNEEYKK
DMAELKQFLE KRSEELFKQY FSKFEELTKL QMESFNQIKN ELRSEMNEIR DEVRSNKLAL
TSEITEEIYP SAPKVSRKQR GVHGFSEPTS EFDFDNSLSL VNENNYDLYE LLDRIINYED
VPLTSSNLFK AEEYQAKVKQ SVYNIKLILK NSEAEATKNY NYILSTLKNE ITLLQKDLPI
ISSQLNKLQH DLRAKQLNRG DYKFVQEQIQ ELRAEHANKT RAISFYNKKV SDLKSIYAQQ
IRKIKSDYKK ISDLANKRKV SSDYIDQALQ SFETARVSQP NIKRNYEQLY RNQLQQNVNA
NYGNFRRYDP LIENHGYEYF SNHQPREFFS ELESIDNDIF SSNDLIYSNR NTYLDENFRI
NDYELTSNFN DIDAIYGMDK LRLPPFEPSN LVNDMEFNSS FDIDFDTDF