ID Q2SKN6_HAHCH Unreviewed; 1651 AA.
AC Q2SKN6;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Alpha-2-macroglobulin {ECO:0000256|PIRNR:PIRNR038980};
GN OrderedLocusNames=HCH_01955 {ECO:0000313|EMBL:ABC28788.1};
OS Hahella chejuensis (strain KCTC 2396).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=349521 {ECO:0000313|EMBL:ABC28788.1, ECO:0000313|Proteomes:UP000000238};
RN [1] {ECO:0000313|EMBL:ABC28788.1, ECO:0000313|Proteomes:UP000000238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2396 {ECO:0000313|EMBL:ABC28788.1,
RC ECO:0000313|Proteomes:UP000000238};
RX PubMed=16352867; DOI=10.1093/nar/gki1016;
RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA Oh T.K., Kim J.F.;
RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT algicidal agent.";
RL Nucleic Acids Res. 33:7066-7073(2005).
CC -!- FUNCTION: Protects the bacterial cell from host peptidases.
CC {ECO:0000256|PIRNR:PIRNR038980}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. Bacterial alpha-2-macroglobulin subfamily.
CC {ECO:0000256|ARBA:ARBA00010556}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000155; ABC28788.1; -; Genomic_DNA.
DR RefSeq; WP_011395859.1; NC_007645.1.
DR STRING; 349521.HCH_01955; -.
DR KEGG; hch:HCH_01955; -.
DR eggNOG; COG2373; Bacteria.
DR HOGENOM; CLU_000965_1_0_6; -.
DR OrthoDB; 9767116at2; -.
DR Proteomes; UP000000238; Chromosome.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:UniProtKB-UniRule.
DR CDD; cd02891; A2M_like; 1.
DR Gene3D; 1.50.10.20; -; 1.
DR Gene3D; 2.60.40.1930; -; 1.
DR InterPro; IPR026284; A2-macglob_dom_prot_bac.
DR InterPro; IPR049120; A2M_bMG2.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR040639; A2MG_MG1.
DR InterPro; IPR047565; Alpha-macroglob_thiol-ester_cl.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR021868; Alpha_2_Macroglob_MG3.
DR InterPro; IPR041203; Bact_A2M_MG5.
DR InterPro; IPR041462; Bact_A2M_MG6.
DR InterPro; IPR041246; Bact_MG10.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR002890; MG2.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR40094; ALPHA-2-MACROGLOBULIN HOMOLOG; 1.
DR PANTHER; PTHR40094:SF1; UBIQUITIN DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF21142; A2M_bMG2; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF17970; bMG1; 1.
DR Pfam; PF17973; bMG10; 1.
DR Pfam; PF11974; bMG3; 1.
DR Pfam; PF17972; bMG5; 1.
DR Pfam; PF17962; bMG6; 1.
DR Pfam; PF01835; MG2; 1.
DR Pfam; PF07678; TED_complement; 1.
DR PIRSF; PIRSF038980; A2M_bac; 1.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SMART; SM01419; Thiol-ester_cl; 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|PIRNR:PIRNR038980};
KW Membrane {ECO:0000256|PIRNR:PIRNR038980};
KW Protease inhibitor {ECO:0000256|PIRNR:PIRNR038980};
KW Reference proteome {ECO:0000313|Proteomes:UP000000238}.
FT DOMAIN 747..893
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 957..1045
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT REGION 25..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1651 AA; 185514 MW; D9A1AC8574AE5976 CRC64;
MREVLTRWAW GLLLVLMVGC SGESGNDDSG KAVQSQAIAE KKASIPTPQP EAKKPPVKVD
RETLKQEYAQ TPFKILRIGE QPWDDGPALS VTFSAPLDQD TMLGRYLTVA DEQNQPVAGD
WILNPVGTTA FFPFVEPERH YTVTVSQGLA AITGRMLEEG ASQQINTRRL DPSVRFISRG
AQLSPELTDG LEIEALNIDA VDIDIWRISD DKMTDFVSGY LGRSYYELEQ LRSWGELVYG
GRFDLNIDVN KRKRRLIDLS SVEPLKQPGI FVAIMKGAGH YPYEYVTTWF TVSDIGLQVR
TYQNQMLAWV NGLADAKPRS GVSIELINQQ GKLLRNAKTD SDGVATFEGA ETSAVLAIAR
TDKQLALVRL NQPAMDLTEF KLPSRKQNPL ELFLYSPRDL YRPGETVHIN ALLRDHDGRK
VTAMPIQAEL TRPDGRVHTS FTWQGDEQSF YTTTFSLPEN TLTGDWFFKA TLGNGDYFLY
RLQVEDFLPE RMRLEIKPDA EHYSTTDTIN LQLQAEYLWG APASGNRAET TLQIAPARTV
SETFSDFIFG EDNDALKETL SLPPVELDEE GRYSLELPNH WSEATMPVRV RANVSVFESG
GRPVARQWQQ SLWPSESLVG VRPLWDGDIA DPETSAAFEL IHINQADELL GMEYLDATLI
REDSAYYWRW SDDGWDYETT ERNQPVYNRV MKIEPGQRLT VSVPVEYGNY RLELRDKQQN
LLNAYKFFAG WSWDGERGGK GPRPEQVELR WDKNAYQGGD TAKLTLQAPF DGRAIVTVEA
NELLWRGAVD VKDGKADINV PVKDIWTRHD MFATALVLRP GKQSALEMPR RAWGMRHLPL
DREARKMQIE LKAPERVEPE SKVAVQIQVQ PGSTASKTVA VTLAAVDTGV LSLTRFKTPD
PFAWFFSPRS YSAEIRDTYS SLIEMSSADR ARQRFGGDAD EMSRGGDAPV SDVQIVSLYS
GKVALDAEGK GTIELQLPYF NGEVRLMAVA FDDARSGSAE KRMTIAAPIV AEINLPRFLA
FGDKTEALWD LQNLLPEQRK LSVKVSADGP LGGAESATEA TLTGKGREWV RLPLEAMDAE
GVGNLSLSVT STDGLEPAIN IQREWKLGLR PPYPAQLNIQ SHVLESSAAM SLTDPLIDVA
LSSSLETQLS VGSVPPLDSN EYMKYLIQYP YGCLEQTSSR VWPLLLATEQ DLFKYDRSSG
KQLAKERDQW IEKGLGRISG MQRYDGSFGL WGNDSDEYHW LSVYATDLLL SAKQRGYNVD
QGLLDNALGR LRTYLTTQGR LSTENSYYSE ARDHYHLAYR AYAALVLASV QQAKLADVRT
LYDNYSKWAK SPLPLAQLAL ALEKLGDARR AQEAWYKALH WGEIGSYYAG DYGSPVRDLA
WTLLLSLDSA VAKQPWDLIY PLRDELRDRR WLSTQEQMAL YRLSLALNSK AGATWKASLA
LNGDSEVLEQ TQQWINTWSK GSWPGDVQLS NMNDFPLFVT FKAQGYPTQA PKPTYDGIEI
ERAFFDLNGQ PLNMKKLESG DFVLVMLQVR SQGNRYLPDA LLVDLLPAGL ELENQNLANA
TRFDEVVVRN KMVRDWVADT RVLHQEYRDD RYVAAVPLDA YSTSVIFYLA RAVSPGEYVI
PPAIVEDMYR PYYRAISDTP GKVTIKERSA Q
//
