ID Q1YJJ0_AURMS Unreviewed; 1826 AA.
AC Q1YJJ0;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE SubName: Full=Putative extracellular alpha-helical protein {ECO:0000313|EMBL:EAS50883.1};
GN ORFNames=SI859A1_01009 {ECO:0000313|EMBL:EAS50883.1};
OS Aurantimonas manganoxydans (strain ATCC BAA-1229 / DSM 21871 / SI85-9A1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Aurantimonadaceae; Aurantimonas.
OX NCBI_TaxID=287752 {ECO:0000313|EMBL:EAS50883.1, ECO:0000313|Proteomes:UP000000321};
RN [1] {ECO:0000313|EMBL:EAS50883.1, ECO:0000313|Proteomes:UP000000321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SI85-9A1 {ECO:0000313|EMBL:EAS50883.1,
RC ECO:0000313|Proteomes:UP000000321};
RX PubMed=18344346; DOI=10.1128/AEM.01656-07;
RA Dick G.J., Podell S., Johnson H.A., Rivera-Espinoza Y., Bernier-Latmani R.,
RA McCarthy J.K., Torpey J.W., Clement B.G., Gaasterland T., Tebo B.M.;
RT "Genomic insights into Mn(II) oxidation by the marine alphaproteobacterium
RT Aurantimonas sp. strain SI85-9A1.";
RL Appl. Environ. Microbiol. 74:2646-2658(2008).
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. Bacterial alpha-2-macroglobulin subfamily.
CC {ECO:0000256|ARBA:ARBA00010556}.
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:EAS50883.1}.
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DR EMBL; AAPJ01000002; EAS50883.1; -; Genomic_DNA.
DR HOGENOM; CLU_000965_1_0_5; -.
DR OrthoDB; 9767116at2; -.
DR BioCyc; AURANTIMONAS:SI859A1_01009-MONOMER; -.
DR Proteomes; UP000000321; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd02891; A2M_like; 1.
DR CDD; cd01100; APPLE_Factor_XI_like; 1.
DR Gene3D; 1.50.10.20; -; 1.
DR Gene3D; 2.60.40.1930; -; 1.
DR Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR026284; A2-macglob_dom_prot_bac.
DR InterPro; IPR049120; A2M_bMG2.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR047565; Alpha-macroglob_thiol-ester_cl.
DR InterPro; IPR021868; Alpha_2_Macroglob_MG3.
DR InterPro; IPR000177; Apple.
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; IPR003609; Pan_app.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
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; 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; PF00024; PAN_1; 1.
DR PIRSF; PIRSF038980; A2M_bac; 1.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SMART; SM00223; APPLE; 1.
DR SMART; SM01419; Thiol-ester_cl; 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000321};
KW Signal {ECO:0000256|SAM:SignalP};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1826
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004197680"
FT DOMAIN 36..101
FT /note="Apple"
FT /evidence="ECO:0000259|SMART:SM00223"
FT REPEAT 226..259
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 960..1104
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 1164..1253
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
SQ SEQUENCE 1826 AA; 193903 MW; 5738929E54C4682B CRC64;
MRGFGRLFFV LAVALLSSGQ ALMPSLAQDG RRVITTEGAD YFGRDYDILK DVDLDQCTAT
CLADDRCQAF TLNTNSRWCF LKEAIGELRT VAGAVSGKVV AEAGIDADSV EARMADLAFL
SAATLDDARQ LRLEIANEDR SIRFGDASAL EIAGLARTAL TQPQAIRAWR EALKRAPLAH
YAWQGIADAA LAYTPEQYGE QPANNRLREA GAINAYLTAG HDDERAAALA TLARAYEAAQ
NWKQAIKAYR ESLALAETGD VRSALDAVVA AHGFRIVDNS VDNNAASPRI CLNFSDALSS
QLTSSENAGD FVQVEGGETL PVTASGSQIC IDGVKHGERY RIVARPGIRS IDGETLSRSA
EVSVYVRDRD PSVRFATNAY VLPAGGEATI PVTTINTDEI EARLQRIGDR ALSRAIADGR
LLQQLSEWQI TEVATETGED VWTGTVGVVR ETNGEVTTAI PVSEIVPEIK PGVYVLTAKA
KNGPQYQDSF ATQWFVVSDI GLTSLAAEDG FHVFARSLGR ADPMAGIRLD LVAANNQVLG
TATTDAAGHA RLPAGLLRGT GGDRPALLTA ARATDDFVFL DLTQTPFDLT DRGVDGRAPA
GPLDVFLTSE RGIYRTGETA FFTGTMRDAT GAAVEGLTMT QIVTRPDGVE HRRRQVADAG
AGGFAFGLDL PAGAMRGVWK VALHTDPKQP ALAETTVIVE DFEPEKIDFE LTTQAEALDP
DAPPVIAVAA RYLFGAPAGG LEVGGEAVLT ATDSLDAYPG YRFGLAGDET TALRQPFNGA
QTDEAGDATI GLDPFPAPAT TKPVTAALQV RVIDTGGRPV ERRLDLPLAG AKPRLGIKPR
FDGTVGEGAE AGFDLIAIDA DGARMAQAGV DWVLNKVNTR FQWYATGGNW NYEPVRSTER
VASGTVDVGT EAPAALSLPV EWGEYELVLS DPSGAAVPAS AGFEAGWYVA AAALDTPDMA
RVSLDKPRYR IGDTAVVRIE PRFAGTAEVL VMDERVITRQ TAEIAAEGGT VELPVTRDWG
PGAYIAAIVY RPMDLDQKRM PGRAIGLAHA EVDPGERALQ VAIAAPEKTE PRQRMTVEVS
VDGVVAGETA YLTLAAVDEG ILNITGFQPP SLSGHYFGKR RLGVDIRDLY SKLIDRMQGA
PGSVRSGGDA GASYDSPPPM EALVALFSGV VTVGADGTVA VPLDIPDFNG TLKLMALAWS
KTGVGEANAS MVVRDPVVIA VNQPRFLAPG DRSRIAIDVT HVEGPTGAAS LAVSGAEGIV
AFDDTAPRRF DLVEGRRETF LMPVTGAAVG DGTLEVALTL PNGDILSKRV TLPVRSIAPE
TVDKSAVTLA ANGGRFDFDR GLFADFLPGT ATATLSVTGA AEFDVAGVVR ALDVYPYGCT
EQITSRAMPL VYLEPTILAA GLNRVEDVKT RVDGAVAGVL ANQSSSGSFG LWRPDYGDLW
LDAYVTDFLT RAREAGYTVP EQGFNLAIDN LRNSLAYLPD APDFGPVAYA SYVLARNGRA
AIGDLRYYAD NELANFRTPL AKAQIGAALA LYGDRVRAER VFRAAVDDAI GSPLLNSQRG
DYGTPLRDDA AILTLGLETA IDGVSFDGLV RQVNDARRTQ RFTSTQEDSW SLLAAHALLD
RSLPKLTVGG RDVDGPYAAA FTAADISGGL DIANRAAEPV RAEITLRGVP EFAPAAQSDG
YAIDRRYYTL DGDPADPSAI GQGERLVTVL EVTLLDSGPA RLMVDDSLPA GFEIDNPAIL
RGGDVAALDW LQLTGEAAHT EFRAERFLAA IDQGDGDTAT RRFAYIVRAV SPGEFVHPAA
LVQNMYDPSR RGRTDEANVS VIGPLR
//
